A5I245 (HIS8_CLOBH) 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:	CBO1571, CLC_1602

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium botulinum › Clostridium botulinum A

Protein attributes

Sequence length	354 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 Reference 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 – 354	354	Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023		PRO_0000319750
Amino acid modifications
	Modified residue	210	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5I245 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: 41EBA5745B7BE4A4	FASTA	354	40,593
	10 20 30 40 50 60 MSKYWSNITK DIEPYVCGEQ PKNKKIIKLN TNENPYPPSP KVLQAIENAA KDDLRLYPDP 70 80 90 100 110 120 NCDTLRKTIA NYYNLSKEEV FIGNGSDEVL SLSFLTFFNP EETVVFSDIS YSFYPVYANL 130 140 150 160 170 180 YKLDYELAKL REDFSIDIED FKNTKGGAII TNPNAPTGLY LSLDSIKQIL EDNINKVVMV 190 200 210 220 230 240 DEAYIDFGGE SSVSLIKDYP NLLVIQTLSK SRSLAGMRIG FALGKKELIE GLNRIKNSFN 250 260 270 280 290 300 SYTIDRISSL AAIEAIKDEE YFKECTLKVI KTRNWTINEL GKIGFKIIPS KANFIFITHD 310 320 330 340 350 TYQAEDILIK LRDENVLVRY FNKDRISNYL RVSIGSKEEM EIFMDKIKKI INKL

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J. Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000727 Genomic DNA. Translation: ABS38142.1. AM412317 Genomic DNA. Translation: CAL83110.1.
RefSeq	YP_001254078.1. NC_009495.1. YP_001387462.1. NC_009698.1.
3D structure databases
ProteinModelPortal	A5I245.
ModBase	Search...
Protein-protein interaction databases
STRING	413999.CBO1571.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS38142; ABS38142; CLC_1602.
GeneID	5185826. 5399619.
KEGG	cbh:CLC_1602. cbo:CBO1571.
PATRIC	19365207. VBICloBot22612_1547.
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HOG000288510.
KO	K00817.
OMA	AHIFHGL.
ProtClustDB	PRK05387.
Enzyme and pathway databases
BioCyc	CBOT413999:GJ72-1629-MONOMER. CBOT441771:GIWX-1570-MONOMER.
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_CLOBH

Accession

Primary (citable) accession number: A5I245
Secondary accession number(s): A7G3U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	June 26, 2007
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program