Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B9L7G2 (HIS4_NAUPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:NAMH_0133
OrganismNautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH) [Complete proteome] [HAMAP]
Taxonomic identifier598659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNautilialesNautiliaceaeNautilia

Protein attributes

Sequence length235 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 – 2352351-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_1000148981

Sites

Active site81Proton acceptor By similarity
Active site1271Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
B9L7G2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 9B7280BAADCD1D1F

FASTA23525,880
        10         20         30         40         50         60 
MIIFPAIDLK DGQAVRLTKG LMDSAKVYSN EPYELAKRFE EMGAEWLHIV DLNGAFAGEP 

        70         80         90        100        110        120 
KNIEQIEKIR KNTNLKIQLG GGIRDEDTIK RYLDLGINRL ILGSIAAKNP KLVSELAEKY 

       130        140        150        160        170        180 
PIAVGIDAKD GFVAIDGWDK TEGILAKDLA EKYKDSKIEC IIATDISKDG TLTGLNIDFI 

       190        200        210        220        230 
LEIQNASQKP VIASGGVASE EDIKKVKENN IYGVIIGKAF YEGKIDLQNV LRENA 

« Hide

References

[1]"Adaptations to submarine hydrothermal environments exemplified by the genome of Nautilia profundicola."
Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.
PLoS Genet. 5:E1000362-E1000362(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1463 / DSM 18972 / AmH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001279 Genomic DNA. Translation: ACM93085.1.
RefSeqYP_002606570.1. NC_012115.1.

3D structure databases

ProteinModelPortalB9L7G2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING598659.NAMH_0133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM93085; ACM93085; NAMH_0133.
GeneID7504474.
KEGGnam:NAMH_0133.
PATRIC22674985. VBINauPro131435_0128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycNPRO598659:GH7N-133-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_NAUPA
AccessionPrimary (citable) accession number: B9L7G2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 37 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