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ECOLI:PUTA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) putA (synonyms: poaA)
Protein Name(s) Bifunctional protein PutA

Proline dehydrogenase Proline oxidase Delta-1-pyrroline-5-carboxylate dehydrogenase P5C dehydrogenase L-glutamate gamma-semialdehyde dehydrogenase

External Links
UniProt P09546
EMBL U05212
U00096
AP009048
X05653
PIR D64843
RefSeq NP_415534.1
YP_489287.1
PDB 1TIW
1TJ0
1TJ1
1TJ2
2AY0
2FZM
2FZN
2GPE
2RBF
3E2Q
3E2R
3E2S
3ITG
4JNY
4JNZ
4O8A
PDBsum 1TIW
1TJ0
1TJ1
1TJ2
2AY0
2FZM
2FZN
2GPE
2RBF
3E2Q
3E2R
3E2S
3ITG
4JNY
4JNZ
4O8A
ProteinModelPortal P09546
SMR P09546
DIP DIP-10620N
IntAct P09546
MINT MINT-1267731
STRING 511145.b1014
DrugBank DB03147
PaxDb P09546
PRIDE P09546
EnsemblBacteria AAC74099
BAA35791
GeneID 12933852
945600
KEGG ecj:Y75_p0987
eco:b1014
PATRIC 32117257
EchoBASE EB0794
EcoGene EG10801
eggNOG COG0506
HOGENOM HOG000253911
InParanoid P09546
KO K13821
OMA PILHVVR
OrthoDB EOG6BS8QW
PhylomeDB P09546
BioCyc EcoCyc:PUTA-MONOMER
ECOL316407:JW0999-MONOMER
MetaCyc:PUTA-MONOMER
RETL1328306-WGS:GSTH-4764-MONOMER
UniPathway UPA00261
UPA00261
EvolutionaryTrace P09546
PRO PR:P09546
Proteomes UP000000318
UP000000625
Genevestigator P09546
GO GO:0009898
GO:0003842
GO:0000986
GO:0001141
GO:0003677
GO:0050660
GO:0016620
GO:0004657
GO:0043565
GO:0045892
GO:0006561
GO:0010133
Gene3D 1.10.2060.10
1.20.5.550
3.20.20.220
3.40.309.10
3.40.605.10
InterPro IPR016161
IPR016163
IPR016160
IPR029510
IPR016162
IPR015590
IPR025703
IPR005933
IPR029041
IPR024090
IPR024089
IPR024082
IPR002872
IPR010985
Pfam PF00171
PF01619
PF14850
PIRSF PIRSF000197
SUPFAM SSF47598
SSF51730
SSF53720
SSF81935
TIGRFAMs TIGR01238
PROSITE PS00070
PS00687

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004657

proline dehydrogenase activity

PMID:22040654[1]

ECO:0000314

F

Table 3 and Figure 3 both show that proline dehydrogenase activity happens here

complete
CACAO 4021

GO:0016020

membrane

PMID:18324349[2]

ECO:0000315

C

Figure 4

complete
CACAO 4026

GO:0004657

proline dehydrogenase activity

PMID:19140736[3]

ECO:0000315

F

Figure 2

complete
CACAO 4028

enables

GO:0004657

proline dehydrogenase activity

PMID:19140736[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004657

proline dehydrogenase activity

PMID:22040654[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:15155740[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004657

proline dehydrogenase activity

PMID:6321477[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010133

proline catabolic process to glutamate

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10801
PANTHER:PTN000193023
SGD:S000001079
UniProtKB:Q9I5F6

P

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10801
PANTHER:PTN000193023

C

Seeded From UniProt

complete

involved_in

GO:0006560

proline metabolic process

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10801
FB:FBgn0037138
PANTHER:PTN000193023
SGD:S000001079
UniProtKB:P10503
UniProtKB:Q9I5F6

P

Seeded From UniProt

complete

enables

GO:0003842

1-pyrroline-5-carboxylate dehydrogenase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10801
PANTHER:PTN000193023
SGD:S000001079
UniProtKB:Q9I5F6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:1618807[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09546

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:12514740[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09546

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:12009917[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09546

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:1618807[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010133

proline catabolic process to glutamate

PMID:7006756[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

PMID:1618807[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004657

proline dehydrogenase activity

PMID:1618807[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003842

1-pyrroline-5-carboxylate dehydrogenase activity

PMID:1618807[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:1618807[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:18586269[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000986

bacterial-type proximal promoter sequence-specific DNA binding

PMID:18586269[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001217

P

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR025703

F

Seeded From UniProt

complete

enables

GO:0003842

1-pyrroline-5-carboxylate dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005933
InterPro:IPR024082
InterPro:IPR024089
InterPro:IPR024090
InterPro:IPR025703

F

Seeded From UniProt

complete

enables

GO:0004657

proline dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR025703

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010985
InterPro:IPR013321
InterPro:IPR025703

P

Seeded From UniProt

complete

involved_in

GO:0006561

proline biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005933

P

Seeded From UniProt

complete

involved_in

GO:0010133

proline catabolic process to glutamate

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR025703

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR029510

F

Seeded From UniProt

complete

enables

GO:0016620

oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016163

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005933
InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR024082
InterPro:IPR024089
InterPro:IPR024090
InterPro:IPR029510

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0006560

proline metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0642

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

involved_in

GO:0010133

proline catabolic process to glutamate

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00261

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Moxley, MA et al. (2011) Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516 113-20 PubMed GONUTS page
  2. Zhou, Y et al. (2008) Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli. Amino Acids 35 711-8 PubMed GONUTS page
  3. 3.0 3.1 Ostrander, EL et al. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry 48 951-9 PubMed GONUTS page
  4. Gu, D et al. (2004) Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme. J. Biol. Chem. 279 31171-6 PubMed GONUTS page
  5. Graham, SB et al. (1984) Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association. J. Biol. Chem. 259 2656-61 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 7.4 7.5 Brown, ED & Wood, JM (1992) Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 13086-92 PubMed GONUTS page
  8. Lee, YH et al. (2003) Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Nat. Struct. Biol. 10 109-14 PubMed GONUTS page
  9. Vinod, MP et al. (2002) Electrochemical and functional characterization of the proline dehydrogenase domain of the PutA flavoprotein from Escherichia coli. Biochemistry 41 6525-32 PubMed GONUTS page
  10. Wood, JM & Zadworny, D (1980) Amplification of the put genes and identification of the put gene products in Escherichia coli K12. Can. J. Biochem. 58 787-96 PubMed GONUTS page
  11. 11.0 11.1 Zhou, Y et al. (2008) Structural basis of the transcriptional regulation of the proline utilization regulon by multifunctional PutA. J. Mol. Biol. 381 174-88 PubMed GONUTS page