Q9S5G6 (HIS8_ECO57) 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:	Z3183, ECs2822

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 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 – 356	356	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153361
Amino acid modifications
	Modified residue	214	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S5G6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 606386762C34FCC0	FASTA	356	39,388
	10 20 30 40 50 60 MSTVTITDLA RENVRNLTPY QSARRLGGNG DVWLNANEYP TAVEFQLTQQ TLNRYPECQP 70 80 90 100 110 120 KAVIENYAQY AGVKPEQVLV SRGADEGIEL LIRAFCEPGK DAILYCPPTY GMYSVSAETI 130 140 150 160 170 180 GVECRTVPTL ENWQLDLQGI SDKLDGVKVV YVCSPNNPTG QLINPQDFRT LLELTRGKAI 190 200 210 220 230 240 VVADEAYIEF CPQASLAGWL AEYPHLAILR TLSKAFALAG LRCGFTLANE EVINLLMKVI 250 260 270 280 290 300 APYPLSTPVA DIAAQALSPQ GIIAMRERVA QIIAEREYLI AALKEIPCVE QVFDSETNYI 310 320 330 340 350 LARFKASSAV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA LRAEQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157." Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y. Microb. Pathog. 26:235-247(1999) [PubMed: 10222209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H- / 184 / EHEC.
[2]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB008676 Genomic DNA. Translation: BAA77744.1. AE005174 Genomic DNA. Translation: AAG57080.1. BA000007 Genomic DNA. Translation: BAB36245.1.
PIR	D85827. F90981.
RefSeq	NP_288526.1. NC_002655.2. NP_310849.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q9S5G6.
SMR	Q9S5G6. Positions 3-356.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000023878; EBESCP00000022771; EBESCG00000022932. EBESCT00000059241; EBESCP00000057069; EBESCG00000058289.
GeneID	914123. 962079.
GenomeReviews	Gene locus Z3183 in contig AE005174_GR. Gene locus ECs2822 in contig BA000007_GR.
KEGG	ece:Z3183. ecs:ECs2822.
PATRIC	18355032. VBIEscCol44059_2717.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008900.
HOGENOM	HBG646350.
OMA	RDQRAVP.
ProtClustDB	PRK01688.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2822-MONOMER.
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

HIS8_ECO57

Accession

Primary (citable) accession number: Q9S5G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program