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Q8GJM0 (HIS4_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:Synpcc7942_1829
ORF Names:sen0020
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

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_0000142064

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Experimental info

Sequence conflict138 – 1458RGWLEDSG → GAAGRFW in AAN46174. Ref.1
Sequence conflict152 – 17524AQQMA…DGTLQ → HSRWQTWRLRTDLHRHWARW HAS in AAN46174. Ref.1
Sequence conflict2251L → F in AAN46174. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8GJM0 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 368F941D8BA49AA7

FASTA25626,326
        10         20         30         40         50         60 
MDVIPAIDLL GGQCVRLFQG DYDQAEVYGK DPVGMALRWA EAGAQRLHLV DLDGAKEGSP 

        70         80         90        100        110        120 
VNAEAIATIA QRLSIPVQVG GGLRDRDTVA RLLDSGVERA ILGTVAVERP ALVEALAGEF 

       130        140        150        160        170        180 
PGQIAVGIDA RSGKVATRGW LEDSGLTAVA LAQQMADLGA CALICTDIGR DGTLQGPNLE 

       190        200        210        220        230        240 
ELRAIAAAVS IPVIASGGVG SLTDLLSLLP LEAQGVSGVI VGKALYTGAV DLQEALRAIG 

       250 
SGRWQDVAVD DSSRLA 

« Hide

References

« Hide 'large scale' references
[1]"Synechococcus elongatus PCC7942 cosmid 4G8."
Holtman C.K., Sandoval P., Chen Y., Socias T., McMurtry S., Gonzalez A., Salinas I., Golden S.S., Youderian P.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY157498 Genomic DNA. Translation: AAN46174.1.
CP000100 Genomic DNA. Translation: ABB57859.1.
RefSeqYP_400846.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ8GJM0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB57859; ABB57859; Synpcc7942_1829.
GeneID3774404.
KEGGsyf:Synpcc7942_1829.
PATRIC23789089. VBISynElo51371_2068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OrthoDBEOG6H1Q3W.
ProtClustDBPRK00748.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1829-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_SYNE7
AccessionPrimary (citable) accession number: Q8GJM0
Secondary accession number(s): Q31M60
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 77 of the entry and version 2 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