Skip Header

Contribute Send feedback
Read comments (?) or add your own

O30725 (HIS4_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. 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
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:RCAP_rcc01154
OrganismRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]
Taxonomic identifier272942 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter ›

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)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.

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2392391-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142044

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Experimental info

Sequence conflict2101D → N in AAC46106. Ref.1
Sequence conflict2181I → F in AAC46106. Ref.1
Sequence conflict223 – 2253IYD → LYN in AAC46106. Ref.1
Sequence conflict2291D → N in AAC46106. Ref.1
Sequence conflict235 – 2395AALKA → RP in AAC46106. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O30725 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: E5ACBE5A88A1ABCC

FASTA23924,468
        10         20         30         40         50         60 
MILYPAIDLK DGNCVRLLHG EMDKATVFGT DPAAQAAKFE AAGCAWVHLV DLNGAFAGEP 

        70         80         90        100        110        120 
VNGAAVEAIL ARITVPAQLG GGIRDMATIE RWLSKGLARV ILGTVAVENP DLVREAAKAF 

       130        140        150        160        170        180 
PGQVAVGIDA RNGKVATKGW ATETDVLVTD LAQSFEDAGV AAIIYTDILR DGAMTGPNIE 

       190        200        210        220        230 
ATEALGRAVT IPVIASGGVS SLPDLIALRD TGVIAGAISG RAIYDGALDL QAALAALKA

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of Rhodobacter capsulatus mutants affected in cytochrome cbb3 oxidase activity."
Koch H.G., Hwang O., Daldal F.
J. Bacteriol. 180:969-978(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MT1131.
[2]"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF016223 Genomic DNA. Translation: AAC46106.1.
CP001312 Genomic DNA. Translation: ADE84912.1.
RefSeqYP_003577319.1. NC_014034.1.

3D structure databases

ProteinModelPortalO30725.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE84912; ADE84912; RCAP_rcc01154.
GeneID9003983.
KEGGrcp:RCAP_rcc01154.
PATRIC35502410. VBIRhoCap134200_1175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000224614.
KOK01814.
OMADGHCVRL.

Enzyme and pathway databases

BioCycRCAP272942:GJIY-1174-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. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00007. TIGR00007. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_RHOCB
AccessionPrimary (citable) accession number: O30725
Secondary accession number(s): D5ARP1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 28, 2011
Last modified: April 3, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents