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

B8JDL2 (HIS4_ANAD2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:A2cp1_0752
OrganismAnaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258) [Complete proteome] [HAMAP]
Taxonomic identifier455488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length238 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 – 2382381-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_1000148947

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
B8JDL2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 77A8CCB0C9170F76

FASTA23824,530
        10         20         30         40         50         60 
MLVIPAIDLI GGEVVRLEKG DFARKTVYAR DPAEKAAELV RDGASLIHVV DLDGAKAGWP 

        70         80         90        100        110        120 
VNLDAVRAIC AVPGAEVELG GGLRSLPDIE KVLELGVRYV VLGTAAVERL DLVRQACARF 

       130        140        150        160        170        180 
PGRVRSGIDA RNGEVKIAGW LEGTGLGAAE VARRVKEAGV GLVEYTDVGR DGMFTGVDAE 

       190        200        210        220        230 
GAARLQAEAG VQVVASGGVA GLDDVRACRA AGLAGVIVGK ALYEGRIALA EAVRAAAE 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Beliaev A.S., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-1 / ATCC BAA-258.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001359 Genomic DNA. Translation: ACL64107.1.
RefSeqYP_002491173.1. NC_011891.1.

3D structure databases

ProteinModelPortalB8JDL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING455488.A2cp1_0752.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL64107; ACL64107; A2cp1_0752.
GeneID7299137.
KEGGacp:A2cp1_0752.
PATRIC20908328. VBIAnaDeh28364_0763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAKIAVSGW.
OrthoDBEOG6H1Q3W.
ProtClustDBCLSK945204.

Enzyme and pathway databases

BioCycADEH455488:GH35-756-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_ANAD2
AccessionPrimary (citable) accession number: B8JDL2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 36 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