Q8Y5X8 (HIS8_LISMO) 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:	lmo1925

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	360 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 Reference 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 – 360	360	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153386
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y5X8 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 6A1CB3E04664BE18	FASTA	360	40,112
	10 20 30 40 50 60 MKWKKSLAGL SSYKPGKREE EVMAELGLTK ITKLSSNENP LGTSPKVAAL QANSNVETEI 70 80 90 100 110 120 YPDGWASSLR KEVTNFYQLE EEELIFTAGV DELIELLTRV LLDTTKNTVM ATPTFVQYRQ 130 140 150 160 170 180 NALIEGAEVR EIPLLTDGAH DLEGMLNAID EKTTIVWICN PNNPTGNYID LADIQAFLDK 190 200 210 220 230 240 VPSDILVVLD EAYIEYVTPQ PKKHEKLIRT YKNLIITRTF SKIYGLASAR VGYGIADKEI 250 260 270 280 290 300 INQLNIVRPP FNTTSIGQKL AIEAIKDQAF IEACRISNAN GIKQYEAFAK RFEQVKLYPA 310 320 330 340 350 360 NGNFVLIDLG IEARTIFSYL EKNGYITRSG AALGFPTAVR ITIGKEEENS AVIALLEKLL

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591981 Genomic DNA. Translation: CAD00003.1.
PIR	AE1315.
RefSeq	NP_465449.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y5X8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	985756.
GenomeReviews	Gene locus lmo1925 in contig AL591824_GR.
KEGG	lmo:lmo1925.
PATRIC	20313045. VBILisMon69206_1971.
Organism-specific databases
GenoList	LMO1925.
Phylogenomic databases
HOGENOM	HBG646350.
OMA	ENPLGMP.
ProtClustDB	PRK03158.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1925-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_LISMO

Accession

Primary (citable) accession number: Q8Y5X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program