A0PP15 (HIS8_MYCUA) 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:	MUL_1573

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium ulcerans

Protein attributes

Sequence length	382 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-Rule MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP-Rule MF_01023
Subunit structure	Homodimer By similarity. HAMAP-Rule 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: 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
Molecule processing
	Chain	1 – 382	382	Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023		PRO_0000319779
Amino acid modifications
	Modified residue	233	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0PP15 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 825BA5936C440434	FASTA	382	40,845
	10 20 30 40 50 60 MTSAPRPRPT LDDLPLREDL RGKSPYGASQ LAVPVRLSTN ENPHPPTQAL VDDVVRSVGE 70 80 90 100 110 120 AAVDLHRYPD RDAVALRTDL ANYLTAQTGT RIGFENVWAA NGSNEILQQL LQAFGGPGRT 130 140 150 160 170 180 AIGFVPSYSM HPIISDGTHT EWVETARADG FGLDIDAAIA VVSDRRPDVV FITSPNNPTG 190 200 210 220 230 240 QSVSLTELRR LLDVVPGILI VDEAYGEFSS QPSAVGLIEE YPTRVVVTRT MSKAFAFAGG 250 260 270 280 290 300 RLGYLVATPA LIDALLLVRL PYHLSSVTQV AARAALRHAQ DTLGSVATLI AERERVSKKL 310 320 330 340 350 360 ASMGFRVIPS DANFVLFGEF ADAPAAWQRY LDQGVLIRDV GIPGYLRATT GLADENDAFL 370 380 RASARIAATD LAPAAASPVG AP

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Agy99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000325 Genomic DNA. Translation: ABL04084.1.
RefSeq	YP_905555.1. NC_008611.1.
3D structure databases
ProteinModelPortal	A0PP15.
SMR	A0PP15. Positions 10-371.
ModBase	Search...
Protein-protein interaction databases
STRING	362242.MUL_1573.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABL04084; ABL04084; MUL_1573.
GeneID	4552309.
KEGG	mul:MUL_1573.
PATRIC	18170059. VBIMycUlc37413_1884.
Organism-specific databases
GenoList	MUL_1573.
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HOG000288510.
KO	K00817.
OMA	GRSAMGF.
ProtClustDB	PRK03317.
Enzyme and pathway databases
UniPathway	UPA00031; UER00012.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_01023. HisC_aminotrans_2.
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
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_MYCUA

Accession

Primary (citable) accession number: A0PP15

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program