Reviewed, UniProtKB/Swiss-Prot Q63XM1 (HIS81_BURPS)

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:	BPSL0518

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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: HAMAP
Molecular function	histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP 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_0000153338
Amino acid modifications
	Modified residue	213	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63XM1-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 2552F2D2AFA5C806	FASTA	356	39,286
	10 20 30 40 50 60 MSRYWSDIVR QLEPYVPGEQ PALAHPVKLN TNENPYPPSP RALDAIRREL GDTGEALRRY 70 80 90 100 110 120 PDPVARRLRE TVAAYHGIAP EQVFAGNGSD EVLAHAFQAL LQHDRPLRFP DITYSFYPTY 130 140 150 160 170 180 ARLYRVAYET VPLADDFSIV VDDYLDDAGC VLFPNPNAPT GRALPLADIE RIVAANPSSV 190 200 210 220 230 240 VVIDEAYVDF GAESAVSLIA RYPNLLVVHT VSKARSLAGM RVGFAFGDAA LIDALTRVKD 250 260 270 280 290 300 SFNSYPLDRL AQVATQASYE DEAWFQATRK QVIASRERLV GALAALGFDV VPSAANFVFA 310 320 330 340 350 RPRSHDAATL AAQLKQREIF VRHFKLPRID QHLRITVGSD AECDALVAAL RELLAA

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571965 Genomic DNA. Translation: CAH34508.1.
RefSeq	YP_107144.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3094062.
GenomeReviews	Gene locus BPSL0518 in contig BX571965_GR.
KEGG	bps:BPSL0518.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63XM1.
OMA	AAYEDDA.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL0518-MON.
BRENDA	2.6.1.9. 275934.
Family and domain databases
HAMAP	MF_01023. [Tree]
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01141. hisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS81_BURPS

Accession

Primary (citable) accession number: Q63XM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)