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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 7 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferaseUniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminaseUniRule annotation
Gene namesi
Name:hisCUniRule annotation
Ordered Locus Names:CBO1571, CLC_1602
OrganismiClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Taxonomic identifieri441771 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000001986 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197501 – 354Histidinol-phosphate aminotransferaseAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei210N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA5I245.
SMRiA5I245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000288510.
KOiK00817.
OMAiPTFDGYP.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiView protein in 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_sub2.
PfamiView protein in Pfam
PF00155. Aminotran_1_2. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiView protein in PROSITE
PS00599. AA_TRANSFER_CLASS_2. 1 hit.

Sequencei

Sequence statusi: Complete.

A5I245-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKYWSNITK DIEPYVCGEQ PKNKKIIKLN TNENPYPPSP KVLQAIENAA
60 70 80 90 100
KDDLRLYPDP NCDTLRKTIA NYYNLSKEEV FIGNGSDEVL SLSFLTFFNP
110 120 130 140 150
EETVVFSDIS YSFYPVYANL YKLDYELAKL REDFSIDIED FKNTKGGAII
160 170 180 190 200
TNPNAPTGLY LSLDSIKQIL EDNINKVVMV DEAYIDFGGE SSVSLIKDYP
210 220 230 240 250
NLLVIQTLSK SRSLAGMRIG FALGKKELIE GLNRIKNSFN SYTIDRISSL
260 270 280 290 300
AAIEAIKDEE YFKECTLKVI KTRNWTINEL GKIGFKIIPS KANFIFITHD
310 320 330 340 350
TYQAEDILIK LRDENVLVRY FNKDRISNYL RVSIGSKEEM EIFMDKIKKI

INKL
Length:354
Mass (Da):40,593
Last modified:June 26, 2007 - v1
Checksum:i41EBA5745B7BE4A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000727 Genomic DNA. Translation: ABS38142.1.
AM412317 Genomic DNA. Translation: CAL83110.1.
RefSeqiWP_011949115.1. NC_009698.1.
YP_001254078.1. NC_009495.1.
YP_001387462.1. NC_009698.1.

Genome annotation databases

EnsemblBacteriaiABS38142; ABS38142; CLC_1602.
GeneIDi5185826.
5399619.
KEGGicbh:CLC_1602.
cbo:CBO1571.
PATRICifig|413999.7.peg.1547.

Similar proteinsi

Entry informationi

Entry nameiHIS8_CLOBH
AccessioniPrimary (citable) accession number: A5I245
Secondary accession number(s): A7G3U7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 26, 2007
Last modified: June 7, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families