A0RBX2 (A0RBX2_BACAH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1 HAMAP MF_01023
EC=2.6.1.9 HAMAP MF_01023

Alternative name(s):
Imidazole acetol-phosphate transaminase 1 HAMAP MF_01023

Gene names

Name:	hisC1 HAMAP MF_01023
Ordered Locus Names:	BALH_1372

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	376 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 SAAS SAAS005861
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023 SAAS SAAS005861
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 SAAS SAAS005861
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP MF_01023 SAAS SAAS005861
Ligand	Pyridoxal phosphate HAMAP MF_01023 SAAS SAAS005861
Molecular function	Aminotransferase HAMAP MF_01023 SAAS SAAS005861 EMBL ABK84715.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP 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
Amino acid modifications
	Modified residue	228	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	A0RBX2 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: BBA9D0DE32FB16EB	FASTA	376	42,261
	10 20 30 40 50 60 MTGGRKMRVK EQLLTLRAYV PGKNIEEVKR EYGLSKIVKL ASNENPFGCS ARVTEALTSL 70 80 90 100 110 120 ASQYALYPDG HAFELRTQVA KHLGVKAEQL LFGSGLDEVI QMISRALLHE GTNVVMANPT 130 140 150 160 170 180 FSQYHHHAVI EGAEVREVSL KDGIHDLDAM LQQVDDQTKI VWICNPNNPT GTYVEKQKLL 190 200 210 220 230 240 SFLESVPKSA LVIMDEAYYE YAGAEDYPRT LPLLEKYENL MVLRTFSKAY GLAAFRIGYA 250 260 270 280 290 300 VGNTELIGQL EVARLPFNTS TVAQSVALAA LEDQAFLQEC VKKNEEGLHQ YYAFCKEYNV 310 320 330 340 350 360 FYYPSQTNFI FLKLGIPGNE AFERLMKKGY IVRSGAAFGI DDGIRITVGL KEENDEIIEL 370 LKELVNEQVQ KEETYS

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK84715.1.
RefSeq	YP_894222.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0RBX2.
ModBase	Search...
Protein-protein interaction databases
STRING	A0RBX2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000068312; EBBACP00000066549; EBBACG00000068303.
GeneID	4545435.
GenomeReviews	Gene locus BALH_1372 in contig CP000485_GR.
KEGG	btl:BALH_1372.
NMPDR	fig|412694.5.peg.1375.
PATRIC	18995140. VBIBacThu63319_1573.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	ENPLGMP.
ProtClustDB	PRK03158.
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

A0RBX2_BACAH

Accession

Primary (citable) accession number: A0RBX2

Entry history

Integrated into UniProtKB/TrEMBL:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)