Reviewed, UniProtKB/Swiss-Prot Q63Q87 (HIS82_BURPS)

Names and origin

Protein names

Recommended name:
    Histidinol-phosphate aminotransferase 2
    EC=2.6.1.9
Alternative name(s):
    Imidazole acetol-phosphate transaminase 2

Gene names

Name:	hisC2
Ordered Locus Names:	BPSL3138

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 2 HAMAP MF_01023		PRO_0000153339
Amino acid modifications
	Modified residue	217	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63Q87-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 6F985612DA171FE7	FASTA	356	38,142
	10 20 30 40 50 60 MTTPEDIIRR DVLAMTGYPV PDATGFVKLD AMENPYSLPA PLAAELGERL AHVALNRYPA 70 80 90 100 110 120 PRPAALIDRL RAVTGVPAAC DVLLGNGSDE IISMLAMACA KPGAKVLAPV PGFVMYELSA 130 140 150 160 170 180 KFAQLEFVGV PLRADLTLDI DAMLAALAEH RPALVYLAYP NNPTGTLYPD EDVERIIAAA 190 200 210 220 230 240 AASLVVIDEA YQPFAQRSWL PRAAQFDNVV VMRTMSKLGL AGIRLGYLVG LPAWLVQFDK 250 260 270 280 290 300 VRPPYNVNVL TQAAAEFLLE RVDVLDAQAA QLRDARTALA HAIGALPGAT VFPSAGNFLL 310 320 330 340 350 VRVPDAAAVF DVLLTERVLI KNVSKMHPLL ANCVRVTVGS PEENARLLAA LKLALP

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: CAH37148.1.
RefSeq	YP_109731.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3092888.
GenomeReviews	Gene locus BPSL3138 in contig BX571965_GR.
KEGG	bps:BPSL3138.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63Q87.
OMA	PEQLLIG.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL3138-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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS82_BURPS

Accession

Primary (citable) accession number: Q63Q87

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 34 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)