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 dehydrogenase

Gene

hisD

Organism
Staphylococcus aureus (strain COL)
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), 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 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei119NADUniRule annotation1
Binding sitei180NADUniRule annotation1
Binding sitei203NADUniRule annotation1
Binding sitei226SubstrateUniRule annotation1
Metal bindingi248ZincUniRule annotation1
Binding sitei248SubstrateUniRule annotation1
Metal bindingi251ZincUniRule annotation1
Binding sitei251SubstrateUniRule annotation1
Active sitei316Proton acceptorUniRule annotation1
Active sitei317Proton acceptorUniRule annotation1
Binding sitei317SubstrateUniRule annotation1
Metal bindingi350ZincUniRule annotation1
Binding sitei350SubstrateUniRule annotation1
Binding sitei404SubstrateUniRule annotation1
Metal bindingi409ZincUniRule annotation1
Binding sitei409SubstrateUniRule 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:SACOL2702
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000530 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358491 – 418Histidinol dehydrogenaseAdd BLAST418

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL2702.

Structurei

3D structure databases

ProteinModelPortaliQ5HCL9.
SMRiQ5HCL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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

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.

Q5HCL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMLNAQQFL NQFSLEAPLD ESLYPIIRDI CQEVKVHGDK ALKMYNLTFD
60 70 80 90 100
HTKTDHLEIS HEQIKAAFDT LDEKTKQALQ QSYERIKAYQ ESIKQTNQQL
110 120 130 140 150
EESVECYEIY HPLESVGIYV PGGKASYPST VLMTATLAQV AGVENIVVVT
160 170 180 190 200
PPQPNGVSQE VLAACYITQV DQVFQVGGAQ SIAALTYGTE TIPKVDKIVG
210 220 230 240 250
PGNQFVAYAK KYLFGQVGID QIAGPTEIAL IIDETADLDA IVYDVFAQAE
260 270 280 290 300
HDELARTYAI SEDAQVLKDL ESRIAKALPN VDRYDIVSKS IANQHYLIHA
310 320 330 340 350
SNFDEACHVM NTIAPEHASI QTVNPQPYIE KVKYVGALFI GHYSPEVIGD
360 370 380 390 400
YVAGPSHVLP TNRTARFTNG LSVNDFLTRN TVIHLSKDTF EQIADSAQHI
410
AHVEALYNHQ QSILIRQS
Length:418
Mass (Da):46,406
Last modified:February 15, 2005 - v1
Checksum:i69AB84E3568981F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW37350.1.

Genome annotation databases

EnsemblBacteriaiAAW37350; AAW37350; SACOL2702.
KEGGisac:SACOL2702.
PATRICi19531652. VBIStaAur112458_2627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW37350.1.

3D structure databases

ProteinModelPortaliQ5HCL9.
SMRiQ5HCL9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL2702.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW37350; AAW37350; SACOL2702.
KEGGisac:SACOL2702.
PATRICi19531652. VBIStaAur112458_2627.

Phylogenomic databases

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

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_STAAC
AccessioniPrimary (citable) accession number: Q5HCL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 86 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

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.