B3R366 (B3R366_CUPTR) 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:	hisC EMBL CAQ68746.1
Synonyms:	hisC1 HAMAP MF_01023
Ordered Locus Names:	RALTA_A0774

Organism

Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]

Taxonomic identifier

164546 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	377 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 CAQ68746.1 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	236	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	B3R366 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: BDC524AB7ADB0C43	FASTA	377	40,419
	10 20 30 40 50 60 MAEQGKQGGA TTVFGPDYVR AISPYVAGKP ISEVAREFGL DEAGIVKLAS NENPLGMPDS 70 80 90 100 110 120 ARAAVAAAVA ELGRYPDANG FALKGALSAR FGVPAEWLTL GNGSNDILEL AAHALVEPGQ 130 140 150 160 170 180 SIVYAEYSFA VYALATQEIG ARAIEVPARD YGHDLDAMAA AIAPDTRLVF IANPNNPTGT 190 200 210 220 230 240 FLPAAQLEAF LQRVPRHVVV VLDEAYNEYL DADQQYDAIA WVRRYPNLLV SRTFSKAYGL 250 260 270 280 290 300 AGLRIGYAVA QPELTDLLNR IRQPFNVNSV AQAAAMAALA DTGFLRRSAE LNRDGKRQLT 310 320 330 340 350 360 EAFDRLGLEY VPSSGNFVLV RVGDDDGAGA HVNLALLRQG VIVRPVGNYN LPRWLRVTIG 370 LPEENAAFIA ALERALA

References

[1]

"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia." Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C. Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU633749 Genomic DNA. Translation: CAQ68746.1.
RefSeq	YP_002004815.1. NC_010528.1.
3D structure databases
ProteinModelPortal	B3R366.
ModBase	Search...
Protein-protein interaction databases
STRING	B3R366.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6454865.
GenomeReviews	Gene locus RALTA_A0774 in contig CU633749_GR.
KEGG	cti:RALTA_A0774.
PATRIC	21528174. VBICupTai42494_0769.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	ENPLGMP.
ProtClustDB	PRK02731.
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

B3R366_CUPTR

Accession

Primary (citable) accession number: B3R366

Entry history

Integrated into UniProtKB/TrEMBL:	September 2, 2008
Last sequence update:	September 2, 2008
Last modified:	December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)