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
Symbiobacterium thermophilum (strain T / IAM 14863)
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:iL-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251NADUniRule annotation
Binding sitei187 – 1871NADUniRule annotation
Binding sitei210 – 2101NADUniRule annotation
Binding sitei233 – 2331SubstrateUniRule annotation
Metal bindingi255 – 2551ZincUniRule annotation
Binding sitei255 – 2551SubstrateUniRule annotation
Metal bindingi258 – 2581ZincUniRule annotation
Binding sitei258 – 2581SubstrateUniRule annotation
Active sitei323 – 3231Proton acceptorUniRule annotation
Active sitei324 – 3241Proton acceptorUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Metal bindingi357 – 3571ZincUniRule annotation
Binding sitei357 – 3571SubstrateUniRule annotation
Binding sitei411 – 4111SubstrateUniRule annotation
Metal bindingi416 – 4161ZincUniRule annotation
Binding sitei416 – 4161SubstrateUniRule 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

BioCyciSTHE292459:GJMM-2938-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:STH2837
OrganismiSymbiobacterium thermophilum (strain T / IAM 14863)
Taxonomic identifieri292459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesSymbiobacteriaceaeSymbiobacterium
ProteomesiUP000000417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Histidinol dehydrogenasePRO_0000135861Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi292459.STH2837.

Structurei

3D structure databases

ProteinModelPortaliQ67KH6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
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.

Q67KH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKVWEPQAF LEFLNRRRTE FYPEIEAQVR AILERVRREG DGALYAFTRQ
60 70 80 90 100
FDGADLEATG LRVTEAEYRE AEAAVSAAFR AALQVAVENI AAFHRPQVPT
110 120 130 140 150
SWFTTRPDGT IVGQRVTPVD RAGVYVPGGS APLFSCLLMT AIPAVVAGVP
160 170 180 190 200
EVIVCTPPDR NGRIDPHMLV AARAAGVKDV YKVGGAQAIG AMAYGTATVP
210 220 230 240 250
RVDKIAGPGN YYVTLAKKLV FGPVGIDMLA GPTEVMAVDD GSVDAEWLAA
260 270 280 290 300
DLLSQAEHPN GMVILVTTAG PERIAAVGAA MARHTAALPR AETIRRSVAE
310 320 330 340 350
LGAALAVDTL EEAADLVNAV GPEHLEVGVA DPWAFLPLVR HAGSIFLGRW
360 370 380 390 400
TPEAMGDYIA GPSNVIPTEG TARYASPVCV ETFIKRSAVT CYSEAAFRAQ
410 420 430
APHAVRLALT EDLLAHAASM QIRLAKPDGE SPSEGREAG
Length:439
Mass (Da):46,628
Last modified:October 11, 2004 - v1
Checksum:i45D8E26BC3568EAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD41822.1.
RefSeqiWP_011196956.1. NC_006177.1.

Genome annotation databases

EnsemblBacteriaiBAD41822; BAD41822; STH2837.
KEGGisth:STH2837.
PATRICi23783855. VBISymThe116959_2816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD41822.1.
RefSeqiWP_011196956.1. NC_006177.1.

3D structure databases

ProteinModelPortaliQ67KH6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292459.STH2837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD41822; BAD41822; STH2837.
KEGGisth:STH2837.
PATRICi23783855. VBISymThe116959_2816.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciSTHE292459:GJMM-2938-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. "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
    Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
    Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: T / IAM 14863.

Entry informationi

Entry nameiHISX_SYMTH
AccessioniPrimary (citable) accession number: Q67KH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 82 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.