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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
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)
  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 sitei125 – 1251NADUniRule annotation
Binding sitei187 – 1871NADUniRule annotation
Binding sitei210 – 2101NADUniRule annotation
Binding sitei234 – 2341SubstrateUniRule annotation
Metal bindingi256 – 2561ZincUniRule annotation
Binding sitei256 – 2561SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule 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

BioCyciBTHE226186:GJXV-202-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:BT_0201
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000001414 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Histidinol dehydrogenasePRO_0000135732Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi226186.BT_0201.

Structurei

3D structure databases

ProteinModelPortaliQ8ABA9.
SMRiQ8ABA9. Positions 7-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
InParanoidiQ8ABA9.
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.

Q8ABA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKLIKYPSK EQWAELLKRP ALNTESLFDT VRTIINKVRA EGDKAVLEYE
60 70 80 90 100
AAFDKVTLSA LTVTSEEIQK AEGLISDELK SAITLAKRNI ETFHSSQRFV
110 120 130 140 150
GKKVETMEGV TCWQKAVGIE KVGLYIPGGT APLFSTVLML AVPAKIAGCR
160 170 180 190 200
EIVLCTPPDK NGNIHPAILF AAQLAGVSKI FKAGGVQAIA AMAYGTESVP
210 220 230 240 250
KVYKIFGPGN QYVTAAKQLV SLRDVAIDMP AGPSEVEVLA DASANPVFVA
260 270 280 290 300
ADLLSQAEHG VDSQAMLITT SEKLQAEVME EVNRQLAKLP RREIAAKSLE
310 320 330 340 350
NSKLILVKDM DEALELTNAY APEHLIVETE NYLEVAERVI NAGSVFLGSL
360 370 380 390 400
TPESAGDYAS GTNHTLPTNG YAKAYSGVSL DSFIRKITFQ EILPQGMKVI
410 420
GPAIEEMAAN ELLDAHKNAV TVRLNTLK
Length:428
Mass (Da):46,246
Last modified:June 6, 2003 - v1
Checksum:i3C7BEEFF3BA154D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO75308.1.
RefSeqiNP_809114.1. NC_004663.1.
WP_011107162.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO75308; AAO75308; BT_0201.
GeneIDi1074912.
KEGGibth:BT_0201.
PATRICi21055143. VBIBacThe70966_0199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO75308.1.
RefSeqiNP_809114.1. NC_004663.1.
WP_011107162.1. NC_004663.1.

3D structure databases

ProteinModelPortaliQ8ABA9.
SMRiQ8ABA9. Positions 7-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226186.BT_0201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO75308; AAO75308; BT_0201.
GeneIDi1074912.
KEGGibth:BT_0201.
PATRICi21055143. VBIBacThe70966_0199.

Phylogenomic databases

eggNOGiCOG0141.
InParanoidiQ8ABA9.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciBTHE226186:GJXV-202-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. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
    Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
    Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Entry informationi

Entry nameiHISX_BACTN
AccessioniPrimary (citable) accession number: Q8ABA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: June 6, 2003
Last modified: May 27, 2015
This is version 98 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.