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A4SG77 (HIS4_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

EC=5.3.1.16
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:hisA
Ordered Locus Names:Cvib_1475
OrganismProsthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides (strain DSM 265)) [Complete proteome] [HAMAP]
Taxonomic identifier290318 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_01014

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2562561-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_1000084104

Sites

Active site81Proton acceptor By similarity
Active site1301Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SG77 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: E74930393473CEFA

FASTA25628,431
        10         20         30         40         50         60 
MLIIPAIDIK DGKCVRLTRG DFSQQKIYLD NPLDMAIIWR KQNAKMLHIV DLDAALTGEM 

        70         80         90        100        110        120 
VNFDIIANIV AELDIPVQIG GGIRSIDAVK RYLDMGVGRV VIGSAAVTDP ELVGELMKHW 

       130        140        150        160        170        180 
PASKIVVGID AENGVPKIKG WTESSGMQDY ELALRMKDMG VERIVYTDIS RDGMMQGFGY 

       190        200        210        220        230        240 
ESTKRFAQKA GLKVTASGGV TNSEDLQRLA TLRPYGVDSV IIGKAFYECN FPCQELWYNF 

       250 
EKGICLDQNF STARRK 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37486.1.
RefSeqYP_001130988.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SG77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37486; ABP37486; Cvib_1475.
GeneID4970135.
KEGGpvi:Cvib_1475.
PATRIC21397454. VBIChlPha132153_1553.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMACARYVVT.
OrthoDBEOG6H1Q3W.
ProtClustDBPRK00748.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1513-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00007. TIGR00007. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_PROVI
AccessionPrimary (citable) accession number: A4SG77
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways