A9IJI5 (A9IJI5_BORPD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 2 HAMAP MF_01023
EC=2.6.1.9 HAMAP MF_01023

Alternative name(s):
Imidazole acetol-phosphate transaminase 2 HAMAP MF_01023

Gene names

Name:	hisC2 HAMAP MF_01023 EMBL CAP42225.1
Ordered Locus Names:	Bpet1886

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	373 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 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 CAP42225.1 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)
	A9IJI5 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: ED13A7AF2D934C3E	FASTA	373	40,108
	10 20 30 40 50 60 MTTAIKPLTA PAHVSAIAPY QAGKPIEELA REFGLDPAGI VKLASNENPL GMPESARHAL 70 80 90 100 110 120 TAAAGTLARY PDPNGFDLKA ALAERYGVPM GWITLGNGSN DILEIAALAL LEPGTSAVYA 130 140 150 160 170 180 QHSFAVYRLA TQARGARHIQ VPARDYGHDL DAMFEAIADD TRLVFIANPN NPTGTFVPGA 190 200 210 220 230 240 DVAAFLQRVH AAHGDRVTVV LDEAYNEYLD PELRFDSVAL VRQYPNLIVS RTFSKAYGLA 250 260 270 280 290 300 GLRVGYAMAQ PALTDLLNRV RQPFNVNTLA QAAAIAALGD ADYLARSYAL NKAGKQQLCA 310 320 330 340 350 360 AFESLARRYV PSYGNFVLVH VGDAQRVNLE LLKRGVIVRP VAGDGLPEWL RVTIGLPEEN 370 QRFIAALTEV LAA

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP42225.1.
RefSeq	YP_001630494.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IJI5.
ModBase	Search...
Protein-protein interaction databases
STRING	A9IJI5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5820416.
GenomeReviews	Gene locus Bpet1886 in contig AM902716_GR.
KEGG	bpt:Bpet1886.
PATRIC	21165231. VBIBorPet31633_1880.
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

A9IJI5_BORPD

Accession

Primary (citable) accession number: A9IJI5

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)