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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
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

Pathway: 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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381NADUniRule annotation
Binding sitei196 – 1961NADUniRule annotation
Binding sitei219 – 2191NADUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Metal bindingi270 – 2701ZincUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Active sitei334 – 3341Proton acceptorUniRule annotation
Active sitei335 – 3351Proton acceptorUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Metal bindingi368 – 3681ZincUniRule annotation
Binding sitei368 – 3681SubstrateUniRule annotation
Binding sitei422 – 4221SubstrateUniRule annotation
Metal bindingi427 – 4271ZincUniRule annotation
Binding sitei427 – 4271SubstrateUniRule annotation

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

BioCyciPATR218491:GJNB-2626-MONOMER.
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:ECA2583
OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Taxonomic identifieri218491 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
ProteomesiUP000007966 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Histidinol dehydrogenasePRO_0000135769Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi218491.ECA2583.

Structurei

3D structure databases

ProteinModelPortaliQ6D411.
SMRiQ6D411. Positions 10-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiIETFHNA.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
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.

Q6D411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNTNSTGS FSTLVDWQRC SVEEQRQLLT RPAISASDRI TAVVSDILTN
60 70 80 90 100
VKSRGDGALR DYSAQFDKVQ VDAIRITDAE IAAASARLGD EVKQAMAIAV
110 120 130 140 150
RNIETFHNAQ KLPIVDIETQ PGVRCQQITR PIATVGLYIP GGSAPLPSTV
160 170 180 190 200
LMLGTPSRIA GCRRVVLCSP PPIADEILYA AQLCGIKEVF QLGGAQAIAA
210 220 230 240 250
MAFGTDSVPK VDKIFGPGNA YVTEAKRQVS QQLDGAAIDM PAGPSEVLVI
260 270 280 290 300
ADSGATPAFV ASDLLSQAEH GPDSQVILLT PDAVMAKAVA DAVEEQLTQL
310 320 330 340 350
SRADIARQAL ASSRVIVARD LAQCIEISNQ YGPEHLIIQT RDAESLVDSI
360 370 380 390 400
TSAGSVFLGD WSPESAGDYA SGTNHVLPTY GYTSTYSSLG LADFQKRMTV
410 420 430 440
QQLTPQGLLQ LAPTIEILAQ AEQLTAHKNA VTLRVAALKE QA
Length:442
Mass (Da):46,850
Last modified:August 16, 2004 - v1
Checksum:i1BE05D0BA8FAC677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950851 Genomic DNA. Translation: CAG75482.1.
RefSeqiWP_011094128.1. NC_004547.2.
YP_050674.1. NC_004547.2.

Genome annotation databases

EnsemblBacteriaiCAG75482; CAG75482; ECA2583.
GeneIDi2882559.
KEGGieca:ECA2583.
PATRICi20480467. VBIPecAtr54885_2617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950851 Genomic DNA. Translation: CAG75482.1.
RefSeqiWP_011094128.1. NC_004547.2.
YP_050674.1. NC_004547.2.

3D structure databases

ProteinModelPortaliQ6D411.
SMRiQ6D411. Positions 10-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi218491.ECA2583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG75482; CAG75482; ECA2583.
GeneIDi2882559.
KEGGieca:ECA2583.
PATRICi20480467. VBIPecAtr54885_2617.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiIETFHNA.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciPATR218491:GJNB-2626-MONOMER.

Family and domain databases

HAMAPiMF_01024. HisD.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCRI 1043 / ATCC BAA-672.

Entry informationi

Entry nameiHISX_PECAS
AccessioniPrimary (citable) accession number: Q6D411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: August 16, 2004
Last modified: April 29, 2015
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

External Data

Dasty 3

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 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.