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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
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 (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 sitei124NADUniRule annotation1
Binding sitei186NADUniRule annotation1
Binding sitei209NADUniRule annotation1
Binding sitei233SubstrateUniRule annotation1
Metal bindingi255ZincUniRule annotation1
Binding sitei255SubstrateUniRule annotation1
Metal bindingi258ZincUniRule annotation1
Binding sitei258SubstrateUniRule annotation1
Active sitei322Proton acceptorUniRule annotation1
Active sitei323Proton acceptorUniRule annotation1
Binding sitei323SubstrateUniRule annotation1
Metal bindingi356ZincUniRule annotation1
Binding sitei356SubstrateUniRule annotation1
Binding sitei410SubstrateUniRule annotation1
Metal bindingi415ZincUniRule annotation1
Binding sitei415SubstrateUniRule 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

BioCyciBFRA272559:GKF0-2949-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:BF3029
OrganismiBacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
Taxonomic identifieri272559 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
Proteomesi
  • UP000006731 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357311 – 428Histidinol dehydrogenaseAdd BLAST428

Interactioni

Protein-protein interaction databases

STRINGi272559.BF3029.

Structurei

3D structure databases

ProteinModelPortaliQ5LAZ8.
SMRiQ5LAZ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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.

Q5LAZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLIKYPDRS QWNEILKRPV LETENLFDTV RNIINRVRAG GDRVVMEYEA
60 70 80 90 100
VFDKAELTSL AVTSAEIEEA EKEVPIELKA AIYLAKRNIE TFHSAQRFEG
110 120 130 140 150
KKVDTMEGVT CWQKAVAIEK VGLYIPGGTA PLFSTVLMLA IPAKIAGCKE
160 170 180 190 200
IVLCTPPDKN GKVHPAILFA ARLAGVSKIF KAGGVQAIAA MAYGTESIPK
210 220 230 240 250
VYKIFGPGNQ YVTAAKQLVS LRDVAIDMPA GPSEVEVLAD ESANPVFVAA
260 270 280 290 300
DLLSQAEHGV DSQAMLVTTS EKLQTEVVYE VERQLGYLTR RDIAEKSLAS
310 320 330 340 350
SKLILVKDME EALELTNAYA PEHLIIETKD YMEVAGQIVN AGSVFLGAFS
360 370 380 390 400
PESAGDYASG TNHTLPTNGY AKAYSGVSLD SFIRKITFQE ILPSGMSAIG
410 420
PAIEVMAANE HLDAHKNAVT VRLEEIRK
Length:428
Mass (Da):46,535
Last modified:June 21, 2005 - v1
Checksum:i731DC2A51FA3930E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR626927 Genomic DNA. Translation: CAH08724.1.
RefSeqiWP_010993237.1. NC_003228.3.

Genome annotation databases

EnsemblBacteriaiCAH08724; CAH08724; BF9343_2943.
KEGGibfs:BF9343_2943.
PATRICi21042676. VBIBacFra29119_3058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR626927 Genomic DNA. Translation: CAH08724.1.
RefSeqiWP_010993237.1. NC_003228.3.

3D structure databases

ProteinModelPortaliQ5LAZ8.
SMRiQ5LAZ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272559.BF3029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH08724; CAH08724; BF9343_2943.
KEGGibfs:BF9343_2943.
PATRICi21042676. VBIBacFra29119_3058.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciBFRA272559:GKF0-2949-MONOMER.

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_BACFN
AccessioniPrimary (citable) accession number: Q5LAZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 21, 2005
Last modified: November 2, 2016
This is version 78 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.