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Q9X0D0 (HIS8_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. 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:
Histidinol-phosphate aminotransferase

EC=2.6.1.9
Alternative name(s):
Imidazole acetol-phosphate transaminase
Gene names
Name:hisC
Ordered Locus Names:TM_1040
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP-Rule MF_01023

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01023

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP-Rule MF_01023

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023
PRO_0000153470

Amino acid modifications

Modified residue2021N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_01023

Secondary structure

......................................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X0D0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: D7CA1B807825376A

FASTA33539,298
        10         20         30         40         50         60 
MNPLDLIAKR AYPYETEKRD KTYLALNENP FPFPEDLVDE VFRRLNSDAL RIYYDSPDEE 

        70         80         90        100        110        120 
LIEKILSYLD TDFLSKNNVS VGNGADEIIY VMMLMFDRSV FFPPTYSCYR IFAKAVGAKF 

       130        140        150        160        170        180 
LEVPLTKDLR IPEVNVGEGD VVFIPNPNNP TGHVFEREEI ERILKTGAFV ALDEAYYEFH 

       190        200        210        220        230        240 
GESYVDFLKK YENLAVIRTF SKAFSLAAQR VGYVVASEKF IDAYNRVRLP FNVSYVSQMF 

       250        260        270        280        290        300 
AKVALDHREI FEERTKFIVE ERERMKSALR EMGYRITDSR GNFVFVFMEK EEKERLLEHL 

       310        320        330 
RTKNVAVRSF REGVRITIGK REENDMILRE LEVFK 

« 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]"Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase."
Fernandez F.J., Vega M.C., Lehmann F., Sandmeier E., Gehring H., Christen P., Wilmanns M.
J. Biol. Chem. 279:21478-21488(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 6-335, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36117.1.
PIRG72304.
RefSeqNP_228846.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H1CX-ray2.85A/B/C/D1-335[»]
1UU0X-ray2.85A/B/C/D1-335[»]
1UU1X-ray2.38A/B/C/D1-335[»]
1UU2X-ray2.80A/B1-335[»]
2F8JX-ray2.40A/B/C/D1-335[»]
ProteinModelPortalQ9X0D0.
SMRQ9X0D0. Positions 1-335.
ModBaseSearch...

Protein-protein interaction databases

STRING243274.TM1040.

Protocols and materials databases

DNASU897350.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36117; AAD36117; TM_1040.
GeneID897350.
KEGGtma:TM1040.
PATRIC23937009. VBITheMar51294_1053.

Phylogenomic databases

eggNOGCOG0079.
KOK00817.
OMAENDMILR.
ProtClustDBPRK14808.

Enzyme and pathway databases

BRENDA2.6.1.9. 6331.
SABIO-RKQ9X0D0.
UniPathwayUPA00031; UER00012.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01023. HisC_aminotrans_2.
InterProIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01141. hisC. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9X0D0.

Entry information

Entry nameHIS8_THEMA
AccessionPrimary (citable) accession number: Q9X0D0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families