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O68602 (HIS4_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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:Cgl2096, cg2299
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length246 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.

Caution

Ala-129 is present instead of the conserved Asp which is expected to be an active site residue.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2462461-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142001

Sites

Active site101Proton acceptor By similarity

Experimental info

Sequence conflict821G → S in AAC05575. Ref.1
Sequence conflict90 – 923ERA → DTQ in AAC05575. Ref.1
Sequence conflict1051A → L in AAC05575. Ref.1
Sequence conflict119 – 1279RYGEKIAVD → AMARRLLS in AAC05575. Ref.1
Sequence conflict1571R → C in AAC05575. Ref.1
Sequence conflict195 – 1984PIVA → TYLT in AAC05575. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O68602 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: 6A35CF9153C32B1E

FASTA24626,609
        10         20         30         40         50         60 
MTFTILPAVD VVNGQAVRLD QGEAGTEKSY GTPLESALKW QEQGAKWLHF VDLDAAFNRG 

        70         80         90        100        110        120 
SNHEMMAEIV GKLDVDVELT GGIRDDESLE RALATGARRV NIGTAALEKP EWIASAIQRY 

       130        140        150        160        170        180 
GEKIAVDIAV RLEDGEWRTR GNGWVSDGGD LWEVLERLDS QGCARFVVTD VSKDGTLSGP 

       190        200        210        220        230        240 
NVELLREVAA ATDAPIVASG GISVLEDVLE LAKYQDEGID SVIIGKALYE HKFTLEEALA 


AVEKLG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum: organization and sequencing analysis of the hisA, impA, and hisF gene cluster."
Jung S.-I., Han M.-S., Kwon J.-H., Cheon C.-I., Min K.-H., Lee M.-S.
Biochem. Biophys. Res. Commun. 247:741-745(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF051846 Genomic DNA. Translation: AAC05575.1.
BA000036 Genomic DNA. Translation: BAB99489.1.
BX927154 Genomic DNA. Translation: CAF20432.1.
PIRJE0213.
RefSeqNP_601295.1. NC_003450.3.
YP_226333.1. NC_006958.1.

3D structure databases

ProteinModelPortalO68602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99489; BAB99489; BAB99489.
CAF20432; CAF20432; cg2299.
GeneID1020047.
3344802.
KEGGcgb:cg2299.
cgl:NCgl2015.
PATRIC21496192. VBICorGlu203724_2032.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMACARYVVT.
OrthoDBEOG6H1Q3W.
ProtClustDBPRK14024.

Enzyme and pathway databases

UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01919. hisA-trpF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_CORGL
AccessionPrimary (citable) accession number: O68602
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 26, 2002
Last modified: February 19, 2014
This is version 102 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