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Q1GHT0 (HIS41_RUEST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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 1

EC=5.3.1.16
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase 1
Gene names
Name:hisA1
Ordered Locus Names:TM1040_1053
OrganismRuegeria sp. (strain TM1040) (Silicibacter sp.) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length247 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 – 2472471-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase 1 HAMAP-Rule MF_01014
PRO_0000290543

Sites

Active site81Proton acceptor By similarity
Active site1281Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GHT0 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 13A0A6887E094FE2

FASTA24726,750
        10         20         30         40         50         60 
MMIYPTMELL DGRCVTLDKG NLDAPMIWHV DPVETAKGFA EAGAEWMHLT DFNALQGDSS 

        70         80         90        100        110        120 
NQDLVEELIR TAGLPIQLGG GIRSREQAEF WIEKGVGRVV IGTMAAYDPA AVAELAKYYP 

       130        140        150        160        170        180 
DQVVLAVDVW QGQVMTEGWR KSGAWTPEAF VKAFGNAPFA GILVTDIDSD MSDLDAQLGL 

       190        200        210        220        230        240 
ISGLAEQAHS PVIASGVVRS KDDISRLKYL PNISGALVGR ALFNKTITLE EAMETAQPNP 


EPVAEFL 

« Hide

References

[1]"Complete sequence of chromosome of Silicibacter sp. TM1040."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000377 Genomic DNA. Translation: ABF63786.1.
RefSeqYP_613048.1. NC_008044.1.

3D structure databases

ProteinModelPortalQ1GHT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292414.TM1040_1053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF63786; ABF63786; TM1040_1053.
GeneID4078111.
KEGGsit:TM1040_1053.
PATRIC23386228. VBIRueSp69653_1939.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OrthoDBEOG6H1Q3W.
ProtClustDBCLSK751584.

Enzyme and pathway databases

BioCycRSP292414:GHCT-1071-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

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

Entry information

Entry nameHIS41_RUEST
AccessionPrimary (citable) accession number: Q1GHT0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 52 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