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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Clostridium botulinum (strain Kyoto / Type A2)
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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:CLM_1812
OrganismiClostridium botulinum (strain Kyoto / Type A2)
Taxonomic identifieri536232 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000001374 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001490871 – 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

ProteinModelPortaliC1FN41.
SMRiC1FN41.
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.

C1FN41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKYWSNITK DIEPYVCGEQ PKNKKIIKLN TNENPYPPSP KVLQAIENAA
60 70 80 90 100
KDDLRLYPDP NCDALRKTIA NYYNLSKEEV FIGNGSDEVL SLSFLTFFNP
110 120 130 140 150
EETIVFSDIS YSFYPVYANL YKLDYKLAKL KEDFSIDIND FKNARGGAVI
160 170 180 190 200
TNPNAPTGVY LSLDSIKQIL EDNINNVVMV DEAYIDFGGE SSVSLIKDYP
210 220 230 240 250
NLLVIQTLSK SRSLAGMRIG FALGQKELIE GLNRIKNSFN SYTIDRISSL
260 270 280 290 300
AAIEAIKDEE YFKECTLKVI KTRNWTINEL GKIGFKIIPS KANFIFITHD
310 320 330 340 350
TYQAEDIFIK LKDENVLVRY FNKDRISNYL RVSIGSKEEM EIFMDKIKKI

INKL
Length:354
Mass (Da):40,494
Last modified:May 26, 2009 - v1
Checksum:i93FF4B3CCD434351
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001581 Genomic DNA. Translation: ACO85753.1.
RefSeqiWP_003358770.1. NC_012563.1.

Genome annotation databases

EnsemblBacteriaiACO85753; ACO85753; CLM_1812.
KEGGicby:CLM_1812.

Similar proteinsi

Entry informationi

Entry nameiHIS8_CLOBJ
AccessioniPrimary (citable) accession number: C1FN41
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: June 7, 2017
This is version 49 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

Documents

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