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

Q8DTR2 (HIS4_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:SMU_1265
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length239 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 – 2392391-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142061

Sites

Active site81Proton acceptor By similarity
Active site1301Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DTR2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: BDCE5748E8BB2472

FASTA23926,013
        10         20         30         40         50         60 
MQILPAIDIK NGHAVRLVKG DFEQETVVND NVLDQASIFM EAGIQYIHVV DLDGALEGRA 

        70         80         90        100        110        120 
ANRDLIAKIK EMTGLAIEVG GGIRTIEQIE DYLSVGINRV IIGSMAVKHP QFVKEALDKF 

       130        140        150        160        170        180 
GSDKIVVGID AKNGMVATEG WLETSTVDYI SLALEMEKMG VRLLIYTDVD RDGTLTGPNF 

       190        200        210        220        230 
EHYEKLIAHL TSAKVIASGG IHALSDLQQL EKIGVAGTIV GKAYYNGDIS LKELREFEG 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58947.1.
RefSeqNP_721641.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DTR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58947; AAN58947; SMU_1265.
GeneID1028554.
KEGGsmu:SMU_1265.
PATRIC19664609. VBIStrMut61772_1134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
KOK01814.
OMACARYVVT.
OrthoDBEOG6H1Q3W.
ProtClustDBPRK00748.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-1200-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_STRMU
AccessionPrimary (citable) accession number: Q8DTR2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 83 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