Q03VY3 (HIS8_LEUMM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase

Gene names

Name:	hisC
Ordered Locus Names:	LEUM_1547

Organism

Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / NCDO 523) [Complete proteome] [HAMAP]

Taxonomic identifier

203120 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Leuconostoc

Protein attributes

Sequence length	357 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
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
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. HAMAP MF_01023
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: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC 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 – 357	357	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000319770
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03VY3 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: F7CA8DE8BC986887	FASTA	357	39,731
	10 20 30 40 50 60 MKKTVKALAA YQAELPVETV KAKYGLQHLA RLSANESVYG PSPKVAQAVR AVSDDILGYY 70 80 90 100 110 120 PDGQATELRE AVAKLNHVDP QHLVFGAGAD ELIELLTRVV LEPGSNIIIP NPTFGEYAMH 130 140 150 160 170 180 AQIEQSTTKK IPVNVDNGNV DFDAILDAID DKTAMVWIAN PNNPTGVFET TSSIKRFLDK 190 200 210 220 230 240 LPANITLVVD EAYYDFVDEP DATVAPLVAE YTNLVVLRTL SKAYGLANLR VGYGIMQDPL 250 260 270 280 290 300 YSAMQAVRLP YNLSTYQIAG GTAAVLDQEY LQKNVQRFQV ERQKFQDFLT KNKFKFYESQ 310 320 330 340 350 ANFIWIKVGE TKKVGQKLLE QGFQVNDRLN PEWIRIALGT PEDNAELKLA FLKATNK

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8293 / NCDO 523.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000414 Genomic DNA. Translation: ABJ62639.1.
RefSeq	YP_819012.1. NC_008531.1.
3D structure databases
ProteinModelPortal	Q03VY3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03VY3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4423277.
GenomeReviews	Gene locus LEUM_1547 in contig CP000414_GR.
KEGG	lme:LEUM_1547.
NMPDR	fig|203120.1.peg.127.
PATRIC	22411075. VBILeuMes50664_1536.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	ECLDASE.
PhylomeDB	Q03VY3.
ProtClustDB	CLSK2319081.
Enzyme and pathway databases
BioCyc	LMES203120:LEUM_1547-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS8_LEUMM

Accession

Primary (citable) accession number: Q03VY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program