Q2L2S9 (Q2L2S9_BORA1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1 HAMAP MF_01023
EC=2.6.1.9 HAMAP MF_01023

Alternative name(s):
Imidazole acetol-phosphate transaminase 1 HAMAP MF_01023

Gene names

Name:	hisC1 HAMAP MF_01023 EMBL CAJ48959.1
Ordered Locus Names:	BAV1350

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 SAAS SAAS005861
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023 SAAS SAAS005861
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 SAAS SAAS005861
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP MF_01023 SAAS SAAS005861
Ligand	Pyridoxal phosphate HAMAP MF_01023 SAAS SAAS005861
Molecular function	Aminotransferase HAMAP MF_01023 SAAS SAAS005861 EMBL CAJ48959.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC 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
Amino acid modifications
	Modified residue	235	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	Q2L2S9 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: E0433649D138EE11	FASTA	373	39,748
	10 20 30 40 50 60 MTQANKTLAA PAHVGAIAPY QAGKPIEELA REFGLDPASI IKLASNENPL GMPESARQAM 70 80 90 100 110 120 LAAAGALARY PDPAGFDLKA ALSARYGVPA NWITLGNGSN DILEIVALAL LAPGRAAVYA 130 140 150 160 170 180 QHSFVVYRLA TQARGARHIM VPAQAYGHDL DAMFAAIDEE TRVVFIANPN NPTGTFAPGA 190 200 210 220 230 240 AIARFLEQVA QAHGERVTVV LDEAYNEYLD PEHRFDSVEL VRRFPNLIVS RTFSKAYGLA 250 260 270 280 290 300 GLRVGFALAQ PALTDLLNRV RQPFNVNTLA QAAAIAALGD AEFLQNAYAT NKAGKAQLCA 310 320 330 340 350 360 AFDKLGLSYV PSYGNFVLVH VGDAPRINLE LLKRGVIVRP VAGDGLPECL RVSIGLPAEN 370 ERFIAALTEI LSA

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM167904 Genomic DNA. Translation: CAJ48959.1.
RefSeq	YP_785872.1. NC_010645.1.
3D structure databases
ProteinModelPortal	Q2L2S9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2L2S9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6267524.
GenomeReviews	Gene locus BAV1350 in contig AM167904_GR.
KEGG	bav:BAV1350.
NMPDR	fig|521.1.peg.519.
PATRIC	21128892. VBIBorAvi43433_1369.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	ENPLGMP.
ProtClustDB	CLSK2332444.
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

Q2L2S9_BORA1

Accession

Primary (citable) accession number: Q2L2S9

Entry history

Integrated into UniProtKB/TrEMBL:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)