A7GN55 (HIS8_BACCN) 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:	Bcer98_1241

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	370 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	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro 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 – 370	370	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_1000084187
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GN55 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 68414178757138A2	FASTA	370	41,937
	10 20 30 40 50 60 MKVKEQLFSL NAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSKRVKEA LALLNEQYAL 70 80 90 100 110 120 YPDGAAFELR QKVANHLKVQ PEQLLFGSGL DEVIQMISRA LLHKGTNVVM ARPTFSQYRH 130 140 150 160 170 180 HAIIEGAEVR EVPLKDGIHD LDAMLEQVDY NTRIVWVCNP NNPTGTYVEK QKLLSFLENV 190 200 210 220 230 240 PKSSLVIMDE AYYEYAGAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAVGYAEL 250 260 270 280 290 300 IKKLEVARLP FNTSTVAQVV ASVAIDDQSF LQECVKKNAE GLEQYYQFCK EYDVFYYPSQ 310 320 330 340 350 360 TNFIFLKIGL PGNEVFERLM KKGYIVRSGA PFGLLDGIRI TVGLKEENAE IIALLANLVK 370 EHVKKEETYS

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS21563.1.
RefSeq	YP_001374558.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GN55.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GN55.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000038063; EBBACP00000037114; EBBACG00000038054.
GeneID	5345180.
GenomeReviews	Gene locus Bcer98_1241 in contig CP000764_GR.
KEGG	bcy:Bcer98_1241.
PATRIC	18930936. VBIBacCyt128034_1312.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	YEYAEAE.
ProtClustDB	PRK03158.
Enzyme and pathway databases
BioCyc	BCER315749:BCER98_1241-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001176. ACC_synthase. 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]
PRINTS	PR00753. ACCSYNTHASE.
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_BACCN

Accession

Primary (citable) accession number: A7GN55

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program