Q31I36 (HIS81_THICR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 1

Gene names

Name:	hisC1
Ordered Locus Names:	Tcr_0591

Organism

Thiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]

Taxonomic identifier

317025 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Histidinol-phosphate aminotransferase 1 HAMAP MF_01023		PRO_0000230225
Amino acid modifications
	Modified residue	210	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q31I36 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 0CB20138F3440893	FASTA	356	39,889
	10 20 30 40 50 60 MSQYWSQLVH TLTPYVPGEQ PKVDNLIKLN TNESPYPPSP LVLNALSSQL NDKLRLYPDP 70 80 90 100 110 120 SSEDLKQSIA TYYGVESNQV FVGNGSDEVL AHAFMTLLKQ DKPILFPDIS YSFYPVYCGL 130 140 150 160 170 180 YEIEHQTIPL TDDFKINPAD YNIENGGIIF PNPNAPTGRL LPLQAIEQIV QQNASSVVVV 190 200 210 220 230 240 DEAYIDFGGE SAAQLVLRYP NLLVVQTFSK SRALAGLRVG FAIGDKALID GLERVKNSFN 250 260 270 280 290 300 SYPLDRLATA GAIAAIEDEP YFQQSCEKII TTRDTLTHFL EDNGFEVIPS AANFVFTRHS 310 320 330 340 350 EMRAEDIANQ LREQAIIVRY FNKPRIDQYL RITIGTEEEN TQLCRALTDI LKTQNA

References

[1]

"The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2." Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., Hauser L.J. , Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., Zeruth G.T. PLoS Biol. 4:1-17(2006) [PubMed: 17105352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: XCL-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000109 Genomic DNA. Translation: ABB41187.1.
RefSeq	YP_390861.1. NC_007520.2.
3D structure databases
ProteinModelPortal	Q31I36.
ModBase	Search...
Protein-protein interaction databases
STRING	Q31I36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3762455.
GenomeReviews	Gene locus Tcr_0591 in contig CP000109_GR.
KEGG	tcx:Tcr_0591.
NMPDR	fig|317025.3.peg.360.
PATRIC	23973086. VBIThiCru83387_0607.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	MKNSFNS.
PhylomeDB	Q31I36.
ProtClustDB	PRK05387.
Enzyme and pathway databases
BioCyc	TCRU317025:TCR_0591-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00817.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01141. HisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS81_THICR

Accession

Primary (citable) accession number: Q31I36

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	December 6, 2005
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program