Q65I37 (HIS8_BACLD) 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:	BLi02397, BL02769

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	361 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.
Sequence caution	The sequence AAU23923.1 differs from that shown. Reason: Erroneous initiation.

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 – 361	361	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153307
Amino acid modifications
	Modified residue	224	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65I37 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: C6E6F90C7C1694DA	FASTA	361	40,337
	10 20 30 40 50 60 MLQIKEQLKQ LTPYQPGKPI EEVKKEFNLD RVVKLASNEN PYGCSEAAKE ALQIEVQQMA 70 80 90 100 110 120 LYPDGYSAAL RTKLASHLGV NETNIILGNG TDEVIQIISR SLLDPASNTV MANPTFSQYK 130 140 150 160 170 180 HNAVIEGAEV REVGLLENGC HDLDAMLKAI DEQTKVVWVC SPNNPTGTYE SGRNLIRFLE 190 200 210 220 230 240 KVPEHVLAVV DEAYYEYVTA EDYPETIPLL ERFPNLMILR TFSKAYGLAS LRVGYGIASE 250 260 270 280 290 300 QLIQAIEPAR QPFNTNRLGQ AAALAALGDQ AFIHDCVRKN NEGLKQYYDF CDEHGLNYYP 310 320 330 340 350 360 SQTNFVLIDF KRDADELFSE LLKKGYIVRS GNALGFPTFL RISVGTKEQN EGFLKTLAGM L

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017333 Genomic DNA. Translation: AAU41277.1. CP000002 Genomic DNA. Translation: AAU23923.1. Different initiation.
RefSeq	YP_079561.1. NC_006270.3. YP_091970.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65I37.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65I37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000057444; EBBACP00000055975; EBBACG00000057435. EBBACT00000058869; EBBACP00000057302; EBBACG00000058860.
GeneID	3027688. 3099452.
GenomeReviews	Gene locus BLi02397 in contig AE017333_GR. Gene locus BL02769 in contig CP000002_GR.
KEGG	bld:BLi02397. bli:BL02769.
NMPDR	fig|279010.5.peg.247.
PATRIC	18950454. VBIBacLic203714_2429.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
PhylomeDB	Q65I37.
ProtClustDB	PRK03158.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02397-MONOMER. BLIC279010:BL02769-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_BACLD

Accession

Primary (citable) accession number: Q65I37
Secondary accession number(s): Q62TI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program