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Q9X0C7 (HIS4_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TM_1037
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Subunit structure

Monomer. Ref.2

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 term3D-structure
Complete proteome
Reference 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 – 2412411-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142068

Sites

Active site81Proton acceptor Probable
Active site1271Proton donor Probable

Experimental info

Mutagenesis81D → N: Loss of activity. Ref.2
Mutagenesis481H → A: Decrease in activity. Ref.2
Mutagenesis511D → N: Decrease in activity. Ref.2
Mutagenesis831R → N: Decrease in activity. Ref.2
Mutagenesis1271D → N: Almost no activity. Ref.2
Mutagenesis1641T → A: Strong decrease in activity. Ref.2

Secondary structure

.................................................. 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X0C7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B1ABDDE5A4D5213D

FASTA24127,028
        10         20         30         40         50         60 
MLVVPAIDLF RGKVARMIKG RKENTIFYEK DPVELVEKLI EEGFTLIHVV DLSNAIENSG 

        70         80         90        100        110        120 
ENLPVLEKLS EFAEHIQIGG GIRSLDYAEK LRKLGYRRQI VSSKVLEDPS FLKSLREIDV 

       130        140        150        160        170        180 
EPVFSLDTRG GRVAFKGWLA EEEIDPVSLL KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT 

       190        200        210        220        230        240 
KKIAIEAEVK VLAAGGISSE NSLKTAQKVH TETNGLLKGV IVGRAFLEGI LTVEVMKRYA 


R 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates."
Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., Sterner R.
Biochemistry 41:12032-12042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, SUBUNIT, MUTAGENESIS OF ASP-8; HIS-48; ASP-51; ARG-83; ASP-127 AND THR-164.
[3]"Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion."
Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.
Science 289:1546-1550(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36114.1.
PIRD72304.
RefSeqNP_228843.1. NC_000853.1.
YP_007977390.1. NC_021214.1.
YP_008991867.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO2X-ray1.85A/B1-241[»]
2CFFX-ray2.50A/B1-241[»]
2W79X-ray1.85A/B1-241[»]
ProteinModelPortalQ9X0C7.
SMRQ9X0C7. Positions 1-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36114; AAD36114; TM_1037.
GeneID897150.
KEGGtma:TM1037.
tmi:THEMA_09175.
tmm:Tmari_1041.
PATRIC23937003. VBITheMar51294_1050.

Phylogenomic databases

eggNOGCOG0106.
KOK01814.
OMAKKENTIF.
OrthoDBEOG6H1Q3W.

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.
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...

Other

EvolutionaryTraceQ9X0C7.

Entry information

Entry nameHIS4_THEMA
AccessionPrimary (citable) accession number: Q9X0C7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 101 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways