Q9X7B8 (HIS8_MYCLE) 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:	ML1258
ORF Names:	MLCB1610.21

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	377 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	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 – 377	377	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153394
Amino acid modifications
	Modified residue	230	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X7B8 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 72190149F6012AE7	FASTA	377	40,351
	10 20 30 40 50 60 MNVPEPTLDD LPLRDNLRGK SPYGAMQLLV PVLLNTNENP HPPTKALVDD VVRSVQKVAV 70 80 90 100 110 120 DLHRYPDRDA VALRQDLASY LTAQTGIRLG VENIWAANGS NEILQQLLQA FGGPGRSAIG 130 140 150 160 170 180 FVPSYSMHPI IADGTHTEWL ETVRADDFSL DVEAAVTAVA DRKPDVVFIA SPNNPSGQSI 190 200 210 220 230 240 SLADLRRLLD VVPGILIVDE AYGEFSSRPS AVALVGEYPT KIVVTRTTSK AFAFAGGRLG 250 260 270 280 290 300 YLIATPALVE AMLLVRLPYH LSSVTQAAAR AALRHADDTL GSVAALIAER ERVTKSLVHM 310 320 330 340 350 360 GFRVIPSDAN FVLFGHFSDA AGAWQHYLDT GVLIRDVGIP GYLRATTGLA EENDAFLKAS 370 SEIAATELAP ATTLGAS

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL049913 Genomic DNA. Translation: CAB43167.1. AL583921 Genomic DNA. Translation: CAC31639.1.
PIR	T45247.
RefSeq	NP_301907.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q9X7B8.
SMR	Q9X7B8. Positions 7-368.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028130; EBMYCP00000027736; EBMYCG00000028125.
GeneID	910368.
GenomeReviews	Gene locus ML1258 in contig AL450380_GR.
KEGG	mle:ML1258.
NMPDR	fig|272631.1.peg.779.
PATRIC	18054760. VBIMycLep78757_2319.
Organism-specific databases
Leproma	ML1258.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00070000031717.
HOGENOM	HBG646350.
OMA	ATATEWV.
ProtClustDB	PRK03317.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1258-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS8_MYCLE

Accession

Primary (citable) accession number: Q9X7B8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program