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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
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 1 (hisG1), ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase 2 (hisG2)
  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 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 sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi361ZincUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei415SubstrateUniRule annotation1
Metal bindingi420ZincUniRule annotation1
Binding sitei420SubstrateUniRule 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:GSU3100
OrganismiGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Taxonomic identifieri243231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
Proteomesi
  • UP000000577 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357741 – 429Histidinol dehydrogenaseAdd BLAST429

Interactioni

Protein-protein interaction databases

STRINGi243231.GSU3100.

Structurei

3D structure databases

ProteinModelPortaliP60859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiP60859.
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.

P60859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFLDIRDTN FDAEFAAILA RGEETGREVE QVVLDIIADV RARGDEALLE
60 70 80 90 100
YTRRFDRLEA DSVAALQVTE DEIEYAFAKV KDEEIAALKL AVERVARFHE
110 120 130 140 150
KQKQETWLST TEPDILLGQM VTPLERVGIY VPGGKASYPS SVIMNAVPAR
160 170 180 190 200
VAGVGEIVMV APTPGGEINP HVLVAARLSG VDRIFRMGGA QAVAALAYGT
210 220 230 240 250
ATVPRVDKIT GPGNIYVATA KKLVFGQVGI DMIAGPSEIL VINDGSGTPA
260 270 280 290 300
HIAADLLSQA EHDELASSIL ITTDRGFGEQ VATEVERQLA QLSRETIART
310 320 330 340 350
SWETYGAVIV AGSLDEAIAF SNRIAPEHLE LAVANPFEIL PRIKNAGAIF
360 370 380 390 400
LGHFTPEAAG DYLAGPNHTL PTGGTARFFS PLSVDDFVKK SSIVYFSAAG
410 420
LNRLGRDIVS IAEMEGLEAH GRSVSIRLK
Length:429
Mass (Da):46,103
Last modified:April 13, 2004 - v1
Checksum:i893372F256C76754
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017180 Genomic DNA. Translation: AAR36491.1.
RefSeqiNP_954141.1. NC_002939.5.
WP_010943721.1. NC_002939.5.

Genome annotation databases

EnsemblBacteriaiAAR36491; AAR36491; GSU3100.
GeneIDi2688475.
KEGGigsu:GSU3100.
PATRICi22029055. VBIGeoSul17553_3124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017180 Genomic DNA. Translation: AAR36491.1.
RefSeqiNP_954141.1. NC_002939.5.
WP_010943721.1. NC_002939.5.

3D structure databases

ProteinModelPortaliP60859.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243231.GSU3100.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAR36491; AAR36491; GSU3100.
GeneIDi2688475.
KEGGigsu:GSU3100.
PATRICi22029055. VBIGeoSul17553_3124.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
InParanoidiP60859.
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_GEOSL
AccessioniPrimary (citable) accession number: P60859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 2, 2016
This is version 92 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.