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MYCTU:O53166

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) acn (ECO:0000313 with EMBL:CCP44235.1)
Protein Name(s) Iron-regulated aconitate hydratase Can (ECO:0000313 with EMBL:AFN49388.1)

Probable iron-regulated aconitate hydratase Acn (Citrate hydro-lyase) (Aconitase) (ECO:0000313 with EMBL:CCP44235.1)

External Links
UniProt O53166
EMBL CP003248
AL123456
JLDD01000018
RefSeq NP_215991.1
YP_006514859.1
ProteinModelPortal O53166
SMR O53166
STRING 83332.Rv1475c
EnsemblBacteria AFN49388
CCP44235
KBJ34833
GeneID 13320068
886545
KEGG mtu:Rv1475c
mtv:RVBD_1475c
PATRIC 18125112
TubercuList Rv1475c
KO K01681
OMA EHVENLA
OrthoDB EOG67DPHM
PhylomeDB O53166
BioCyc MetaCyc:MONOMER-11945
Proteomes UP000001584
UP000003123
GO GO:0005618
GO:0005829
GO:0005576
GO:0005886
GO:0003994
GO:0030350
GO:0040007
GO:0010039
Gene3D 3.20.19.10
3.30.499.10
3.40.1060.10
InterPro IPR015931
IPR015937
IPR001030
IPR015928
IPR015934
IPR015932
IPR018136
IPR000573
PANTHER PTHR11670
PTHR11670:SF1
Pfam PF00330
PF00694
PRINTS PR00415
SUPFAM SSF52016
SSF53732
PROSITE PS00450
PS01244

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003994

aconitate hydratase activity

PMID:17384188[1]

ECO:0000314

F

purified protein with assay

complete

GO:0005506

iron ion binding

PMID:17384188[1]

ECO:0000314

F

Source: UniProtKB-KW; Purified the protein and showed that the activity of the protein was lost in the presences of an iron chelator.

complete

enables

GO:0003730

mRNA 3'-UTR binding

PMID:17384188[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003729

mRNA binding

PMID:17384188[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P09339

F

Seeded From UniProt

complete

enables

GO:0047456

2-methylisocitrate dehydratase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q8ZP52

F

Seeded From UniProt

complete

enables

GO:0030350

iron-responsive element binding

PMID:17384188[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010039

response to iron ion

PMID:9864233[2]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:15525680[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:14532352[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15525680[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:15525680[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:17443846[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003994

aconitate hydratase activity

PMID:17384188[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11325
PANTHER:PTN000186700
RGD:621539
UniProtKB:P09339
UniProtKB:P21399
UniProtKB:Q0VCU1

F

Seeded From UniProt

complete

involved_in

GO:0006101

citrate metabolic process

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000186700
TAIR:locus:2116297
UniProtKB:P21399
UniProtKB:Q0VCU1
UniProtKB:Q42560

P

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000186700
UniProtKB:Q8ZP52

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11325
MGI:MGI:1928268
MGI:MGI:87879
PANTHER:PTN000186700
RGD:2019
RGD:621539
UniProtKB:P21399
UniProtKB:Q42560
UniProtKB:Q8IDR8
WB:WBGene00000040

C

Seeded From UniProt

complete

enables

GO:0003994

aconitate hydratase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11325
FB:FBgn0024957
FB:FBgn0024958
MGI:MGI:87879
PANTHER:PTN000186700
RGD:2019
TAIR:locus:2063354
TAIR:locus:2116297
UniProtKB:P09339
UniProtKB:P21399
UniProtKB:Q0VCU1
UniProtKB:Q42560
UniProtKB:Q8IDR8
UniProtKB:Q8ZP52
WB:WBGene00000040

F

Seeded From UniProt

complete

enables

GO:0003994

aconitate hydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.3

F

Seeded From UniProt

complete

enables

GO:0047456

2-methylisocitrate dehydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.99

F

Seeded From UniProt

complete

involved_in

GO:0019679

propionate metabolic process, methylcitrate cycle

PMID:17384188[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:17384188[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0816
UniPathway:UPA00223

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Banerjee, S et al. (2007) Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase. J. Bacteriol. 189 4046-52 PubMed GONUTS page
  2. Wong, DK et al. (1999) Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect. Immun. 67 327-36 PubMed GONUTS page
  3. 3.0 3.1 3.2 Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
  4. Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
  5. Målen, H et al. (2007) Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7 1702-18 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page