Reviewed, UniProtKB/Swiss-Prot Q7WDY3 (HIS82_BORBR)

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:	BB4855

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	365 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 – 365	365	Histidinol-phosphate aminotransferase 2 HAMAP MF_01023		PRO_0000153320
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WDY3-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: B4DE67CE9944B103	FASTA	365	38,985
	10 20 30 40 50 60 MTGVAAPERI ARAVRADIRA LTAYPVADAA GCIKLDAMEC PYELPAEVRD DIARAARETP 70 80 90 100 110 120 LNRYPAAANP ALQAQVRQAF EVPAQAGLLF GNGSDELIHL IIQACCEPGD TVLSPWPSFV 130 140 150 160 170 180 YFDMAARLSH ARFVGVPLTA GLELDLPATL AAIEAHQPKV VFLALPNNPT GGLWPDAAVR 190 200 210 220 230 240 AILDAAPGLV VLDEAYQPFA GHTWMPRIMD EPNAVVMRTV SKIGLAGLRF GYLAGHPAWI 250 260 270 280 290 300 AEFDKVRPPY NMDVLSQAVL AAVLRHKPVL DAQADRLRAD RQPLADGLAA LPGVTVFPSA 310 320 330 340 350 360 GNFVLARFCG KLDGNAVHLA LKTRKILVRN FSNAHPLLAD CLRISVGTPT ENAAVLSALQ DILSA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640451 Genomic DNA. Translation: CAE35218.1.
RefSeq	NP_891388.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2659706.
GenomeReviews	Gene locus BB4855 in contig BX470250_GR.
KEGG	bbr:BB4855.
NMPDR	fig|257310.1.peg.4835.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WDY3.
OMA	PEQLLIG.
Enzyme and pathway databases
BioCyc	BBRO257310:BB4855-MON.
BRENDA	2.6.1.9. 413.
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_BORBR

Accession

Primary (citable) accession number: Q7WDY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 41 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)