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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Shewanella sediminis (strain HAW-EB3)
Status
Unreviewed-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 annotationSAAS annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotationSAAS 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 annotationSAAS 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. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  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 sitei127NADUniRule annotation1
Binding sitei185NADUniRule annotation1
Binding sitei208NADUniRule annotation1
Binding sitei235SubstrateUniRule annotation1
Metal bindingi257ZincUniRule annotation1
Binding sitei257SubstrateUniRule annotation1
Metal bindingi260ZincUniRule annotation1
Binding sitei260SubstrateUniRule annotation1
Active sitei324Proton acceptorUniRule annotation1
Active sitei325Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi358ZincUniRule annotation1
Binding sitei358SubstrateUniRule annotation1
Binding sitei412SubstrateUniRule annotation1
Metal bindingi417ZincUniRule annotation1
Binding sitei417SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

Metal-bindingUniRule annotationSAAS annotation, NADUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotationSAAS annotation (EC:1.1.1.23UniRule annotationSAAS annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:Ssed_2542Imported
OrganismiShewanella sediminis (strain HAW-EB3)Imported
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002015 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi425104.Ssed_2542.

Structurei

3D structure databases

ProteinModelPortaliA8FWC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotationSAAS 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.

A8FWC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQILNWASLT DTDRKAALSR SPLVGDASLE QDVLAIVNEV QIGKDAALKD
60 70 80 90 100
YSRKFDGVTV EQLKLSEGDI DAACARVDEE IKLAVSQAIT NIDTFHQAQK
110 120 130 140 150
FEPVNIETQK GIRCELRSEP IEKVGLYIPG GSAPLISTVL MLALPAKIAG
160 170 180 190 200
CEQRVLVSPP PINDAIVYAA NACGITEILQ VGGAQAIAAL AFGTESVPAV
210 220 230 240 250
DKIFGPGNRY VTEAKRIVSQ DSRCVVSIDM PAGPSEVLLI ADSDANAEFI
260 270 280 290 300
AADLLSQAEH GPDSQVMLVT DCSALADEVN LALARQLELL PRVDIAEVAL
310 320 330 340 350
ESSRTLLVEN MEQAAQVSNL YGPEHLIIQT QNPREVLKQI RAAGSVFLGA
360 370 380 390 400
YTPESVGDYA SGTNHVLPTY GYSRAVSSLS LADFSRRFTV QELSAEGLIG
410 420 430
LSQTVMTLAA AEQLDAHKNA VAIRIASLQS DVAAQAKGV
Length:439
Mass (Da):46,674
Last modified:November 13, 2007 - v1
Checksum:i1FA189C96C78C7EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37149.1.
RefSeqiWP_012142882.1. NC_009831.1.

Genome annotation databases

EnsemblBacteriaiABV37149; ABV37149; Ssed_2542.
KEGGisse:Ssed_2542.
PATRICi23562755. VBISheSed62411_2716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37149.1.
RefSeqiWP_012142882.1. NC_009831.1.

3D structure databases

ProteinModelPortaliA8FWC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi425104.Ssed_2542.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV37149; ABV37149; Ssed_2542.
KEGGisse:Ssed_2542.
PATRICi23562755. VBISheSed62411_2716.

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 nameiA8FWC6_SHESH
AccessioniPrimary (citable) accession number: A8FWC6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: November 2, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.