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ECOLI:HEM3

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) hemC (synonyms: popE)
Protein Name(s) Porphobilinogen deaminase

PBG Hydroxymethylbilane synthase HMBS Pre-uroporphyrinogen synthase

External Links
UniProt P06983
EMBL X04242
X12614
M87049
U00096
AP009048
X66782
PIR F65184
RefSeq YP_026260.1
YP_491637.1
PDB 1AH5
1GTK
1PDA
1YPN
2YPN
PDBsum 1AH5
1GTK
1PDA
1YPN
2YPN
ProteinModelPortal P06983
SMR P06983
DIP DIP-9879N
IntAct P06983
MINT MINT-1302039
STRING 511145.b3805
PaxDb P06983
PRIDE P06983
EnsemblBacteria AAT48218
BAE77496
GeneID 12930663
947759
KEGG ecj:Y75_p3373
eco:b3805
PATRIC 32123109
EchoBASE EB0424
EcoGene EG10429
eggNOG COG0181
HOGENOM HOG000228588
InParanoid P06983
KO K01749
OMA GIECRTD
OrthoDB EOG6HB9Z6
PhylomeDB P06983
BioCyc EcoCyc:OHMETHYLBILANESYN-MONOMER
ECOL316407:JW5932-MONOMER
MetaCyc:OHMETHYLBILANESYN-MONOMER
UniPathway UPA00251
EvolutionaryTrace P06983
PRO PR:P06983
Proteomes UP000000318
UP000000625
Genevestigator P06983
GO GO:0005737
GO:0004418
GO:0006783
GO:0018160
GO:0006782
GO:0033014
Gene3D 3.30.160.40
HAMAP MF_00260
InterPro IPR000860
IPR022419
IPR022417
IPR022418
PANTHER PTHR11557
Pfam PF01379
PF03900
PIRSF PIRSF001438
PRINTS PR00151
SUPFAM SSF54782
TIGRFAMs TIGR00212
PROSITE PS00533

Annotations

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

NOT

GO:0004418

hydroxymethylbilane synthase activity

PMID:1747120[1]

ECO:0000315

F

Fig. 2 shows a liquid chromatography column of mutants. Fig. 2b specifically shows that the RH11 mutant cannot create the enzyme-intermediate needed to catalyze the reaction.

complete
CACAO 4661

involved_in

GO:0006783

heme biosynthetic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10429
PANTHER:PTN000168159
SGD:S000002364
UniProtKB:Q8I5V3

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10429
PANTHER:PTN000168159
RGD:2801

C

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10429
PANTHER:PTN000168159
RGD:2801
SGD:S000002364
TAIR:locus:2150758
UniProtKB:P08397

F

Seeded From UniProt

complete

involved_in

GO:0033014

tetrapyrrole biosynthetic process

PMID:379277[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0018160

peptidyl-pyrromethane cofactor linkage

PMID:8727319[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006783

heme biosynthetic process

PMID:379277[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:3052434[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

PMID:379277[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006782

protoporphyrinogen IX biosynthetic process

PMID:8224882[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

PMID:3052434[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000860
InterPro:IPR022417
InterPro:IPR022418
InterPro:IPR022419
InterPro:IPR036803

F

Seeded From UniProt

complete

involved_in

GO:0018160

peptidyl-pyrromethane cofactor linkage

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022419

P

Seeded From UniProt

complete

involved_in

GO:0033014

tetrapyrrole biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000860
InterPro:IPR022417
InterPro:IPR022418
InterPro:IPR022419
InterPro:IPR036803

P

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.5.1.61

F

Seeded From UniProt

complete

involved_in

GO:0006779

porphyrin-containing compound biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083066

P

Seeded From UniProt

complete

enables

GO:0004418

hydroxymethylbilane synthase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083066

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0006779

porphyrin-containing compound biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0627

P

Seeded From UniProt

complete

involved_in

GO:0006782

protoporphyrinogen IX biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00251

P

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ Jordan, PM & Woodcock, SC (1991) Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. Biochem. J. 280 ( Pt 2) 445-9 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 McConville, ML & Charles, HP (1979) Mutants of Escherichia coli K12 accumulating porphobilinogen: a new locus, hemC. J. Gen. Microbiol. 111 193-200 PubMed GONUTS page
  4. ↑ Louie, GV et al. (1996) The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution. Proteins 25 48-78 PubMed GONUTS page
  5. ↑ 5.0 5.1 Jordan, PM et al. (1988) Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. Biochem. J. 254 427-35 PubMed GONUTS page
  6. ↑ Nishimura, K et al. (1993) Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12. Gene 133 109-13 PubMed GONUTS page
  7. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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