Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Status
Reviewed-Annotation score: -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 (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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

BioCyciDHAF272564:G1GUH-1527-MONOMER
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:Dhaf_1493
OrganismiDesulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Taxonomic identifieri272564 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
Proteomesi
  • UP000007726 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001490921 – 360Histidinol-phosphate aminotransferaseAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB8FP20
SMRiB8FP20
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
OMAiKYKMDAN

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01023 HisC_aminotrans_2, 1 hit
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR005861 HisP_aminotrans
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01141 hisC, 1 hit

Sequencei

Sequence statusi: Complete.

B8FP20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDKMNLEEW MRPSIRTLKA YESKSIPDCV RLDANENPLP WPPGMIEQLL
60 70 80 90 100
GSAIAFNRYP DGGAQELKEA LSRYTGVPAE GILTGNGSDE LIQLLMTTFG
110 120 130 140 150
GEKGAVVIHP PTFSMYEAAA RVTGTEVLEV PLLLTETSRD FRLDVEGILK
160 170 180 190 200
AAAQPQVHMI VLCNPNNPTG TLFPREEILR IVAESGKIVI VDEAYGEFSG
210 220 230 240 250
ESVVDQIPYC PNLLVMKTFS KLFAMAALRL GYLLGQPSII GALNRARQPF
260 270 280 290 300
NVNSFSQKAG VIALNYGEEY AEQGRILIAE LARIAEALTA FASVKVFATR
310 320 330 340 350
ANFLLFQPED PDRVYQELIG KGFLIRTMGN LPLVGKALRL STGLPEENER
360
LIKALGEILK
Length:360
Mass (Da):39,525
Last modified:March 3, 2009 - v1
Checksum:iE087B1FE2A09EAFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001336 Genomic DNA Translation: ACL19545.1
RefSeqiWP_015943472.1, NC_011830.1

Genome annotation databases

EnsemblBacteriaiACL19545; ACL19545; Dhaf_1493
KEGGidhd:Dhaf_1493

Similar proteinsi

Entry informationi

Entry nameiHIS8_DESHD
AccessioniPrimary (citable) accession number: B8FP20
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 25, 2018
This is version 56 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health