Q81C43 (HIS82_BACCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 2
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 2

Gene names

Name:	hisC2
Ordered Locus Names:	BC_2940

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	366 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 – 366	366	Histidinol-phosphate aminotransferase 2 HAMAP MF_01023		PRO_0000153302
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81C43 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A8BBBC691E43DD49	FASTA	366	41,308
	10 20 30 40 50 60 MQVKDQLSSL QPYKPGKSPE QMKEVYGDHS FVKLASNENP FGCSPRVLDE LQKSWLEHAL 70 80 90 100 110 120 YPDGGATTLR QIIADKLHVK MEQVLCGSGL DEIIQIISRA VLRAGDNIVT AGATFPQYRH 130 140 150 160 170 180 HAIIEGCEVK EVALNNGVYD LEEISSVVDN DTKIVWICNP NNPTGTYVND RKLTQFIEGI 190 200 210 220 230 240 SENTLIVIDE AYYEYVTAKD FPETLPLLEK HKNILVLRTF SKAYGLASFR VGYAVGQEEL 250 260 270 280 290 300 IEKLNVVRLP FNVSSLAQKA ATIAFGDDEF IEEIVRVNTE GLQQYESFCR ENDIPFYPSQ 310 320 330 340 350 360 TNFIFLPVEN AREIYEACAH AGFIIRPFPN GIRITVGTRE QNEGVISVLQ QHFENKKRKS RDEENA

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP09888.1.
RefSeq	NP_832687.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q81C43.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81C43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000034282; EBBACP00000033488; EBBACG00000034273.
GeneID	1205288.
GenomeReviews	Gene locus BC_2940 in contig AE016877_GR.
KEGG	bce:BC2940.
PATRIC	32601821. VBIBacCer54481_3015.
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	NNTKIVW.
PhylomeDB	Q81C43.
ProtClustDB	PRK01533.
Enzyme and pathway databases
BioCyc	BCER226900:BC_2940-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

HIS82_BACCR

Accession

Primary (citable) accession number: Q81C43

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program