A7ZNJ3 (HIS8_ECO24) 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:	EcE24377A_2312

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [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_1000063473
Amino acid modifications
	Modified residue	214	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZNJ3 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 36FB3343CD89A5E6	FASTA	356	39,450
	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 DNWQLDLQGI SDKLDGVKVV YVCSPNNPTG QLINPQDFRT LLELTRGKAI 190 200 210 220 230 240 VVADEAYIEF CPQASLTGWL AEYPHLAILR TLSKAFALAG LRCGFTLANE EVINLLMKVI 250 260 270 280 290 300 APYPLSTPVA DIAAQALSPQ GIVAMRERVT QIIAEREYLI AALKEIPCVE QVFDSETNYI 310 320 330 340 350 LARFKASSTV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA LRAEQV

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV17866.1.
RefSeq	YP_001463372.1. NC_009801.1.
3D structure databases
ProteinModelPortal	A7ZNJ3.
SMR	A7ZNJ3. Positions 3-356.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZNJ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000021546; EBESCP00000020608; EBESCG00000020600.
GeneID	5586045.
GenomeReviews	Gene locus EcE24377A_2312 in contig CP000800_GR.
KEGG	ecw:EcE24377A_2312.
NMPDR	fig|331111.3.peg.55.
PATRIC	18293897. VBIEscCol31211_2593.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000008900.
HOGENOM	HBG646350.
OMA	RDQRAVP.
ProtClustDB	PRK01688.
Enzyme and pathway databases
BioCyc	ECOL331111:ECE24377A_2312-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_ECO24

Accession

Primary (citable) accession number: A7ZNJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program