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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 9 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)
  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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116NADUniRule annotation1
Binding sitei177NADUniRule annotation1
Binding sitei200NADUniRule annotation1
Binding sitei223SubstrateUniRule annotation1
Metal bindingi245ZincUniRule annotation1
Binding sitei245SubstrateUniRule annotation1
Metal bindingi248ZincUniRule annotation1
Binding sitei248SubstrateUniRule annotation1
Active sitei313Proton acceptorUniRule annotation1
Active sitei314Proton acceptorUniRule annotation1
Binding sitei314SubstrateUniRule annotation1
Metal bindingi347ZincUniRule annotation1
Binding sitei347SubstrateUniRule annotation1
Binding sitei401SubstrateUniRule annotation1
Metal bindingi406ZincUniRule annotation1
Binding sitei406SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:SSP0429
OrganismiStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Taxonomic identifieri342451 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000006371 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358571 – 423Histidinol dehydrogenaseAdd BLAST423

Interactioni

Protein-protein interaction databases

STRINGi342451.SSP0429.

Structurei

3D structure databases

ProteinModelPortaliQ4A044.
SMRiQ4A044.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4A044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIDKTLFLK KYLNQSSLNE DLYPIVKDIC ENVRLHGDDA LRNYNQQFDQ
60 70 80 90 100
VETCNLEVAY QTLENAYNRL DSDLREALQQ SHARIQSYQE SIKWTKQQGT
110 120 130 140 150
SDCYELYHPL ERVGVYVPGG KASYPSTVLM TVTLAKVAGV KNISVVTPPQ
160 170 180 190 200
LNGIPDIVLA ACYIAGVDNV YQVGGAQSIA ALAYGTETLP KVDKIVGPGN
210 220 230 240 250
QFVAYAKKYL FGQVGIDQIA GPSEIALIID DSADLDAIAY DVFAQAEHDE
260 270 280 290 300
LARTFVISED EALLKQLEQK IQHILPQIER QSIVQASLND NHFLIHVNNF
310 320 330 340 350
SEACDLMNQI APEHASIQTV SPHDYLNHVR YVGALFLGYY SPEVIGDYVA
360 370 380 390 400
GPSHVLPTNQ TARFTNGLSV NDFLTRHSVI DLSKDTFDTV ELTARKLAHV
410 420
EQLYNHEQSI EIRTSKEFND DKN
Length:423
Mass (Da):47,268
Last modified:September 13, 2005 - v1
Checksum:iAD6BEF5C7FA5E229
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17574.1.

Genome annotation databases

EnsemblBacteriaiBAE17574; BAE17574; SSP0429.
KEGGissp:SSP0429.
PATRICi19622347. VBIStaSap90642_0434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17574.1.

3D structure databases

ProteinModelPortaliQ4A044.
SMRiQ4A044.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342451.SSP0429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE17574; BAE17574; SSP0429.
KEGGissp:SSP0429.
PATRICi19622347. VBIStaSap90642_0434.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_STAS1
AccessioniPrimary (citable) accession number: Q4A044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: September 13, 2005
Last modified: November 2, 2016
This is version 81 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.