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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Mycobacterium smegmatis
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.By similarity

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

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.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. Phosphoribosyl isomerase A (priA_2)
  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), Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hpsN_3), Histidinol dehydrogenase (hpsN_2), Histidinol dehydrogenase (hpsN_1), Histidinol dehydrogenase (hisD), 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 sitei136NADBy similarity1
Binding sitei200NADBy similarity1
Binding sitei228NADBy similarity1
Binding sitei251SubstrateBy similarity1
Metal bindingi273ZincBy similarity1
Binding sitei273SubstrateBy similarity1
Metal bindingi276ZincBy similarity1
Binding sitei276SubstrateBy similarity1
Active sitei342Proton acceptorBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei343SubstrateBy similarity1
Metal bindingi376ZincBy similarity1
Binding sitei376SubstrateBy similarity1
Binding sitei430SubstrateBy similarity1
Metal bindingi435ZincBy similarity1
Binding sitei435SubstrateBy similarity1

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 dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
OrganismiMycobacterium smegmatis
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357981 – 445Histidinol dehydrogenaseAdd BLAST445

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_3205.

Structurei

3D structure databases

ProteinModelPortaliP28736.
SMRiP28736.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.

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.

P28736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMMAKFQMS RIDLRNRVLS AAQLRSALPR GGVDVDAVVP KVRPIVDAVA
60 70 80 90 100
QRGAQAALEY GESFDGIRPE TVRVPRELLS QALENLDADV RAALQVSIDR
110 120 130 140 150
ARAVHADQRR TDTTTTLAPG ATVTERWVPV ERVGLYVPGG NAVYPSSVVM
160 170 180 190 200
NVVPAQTAGV DSMVIASPPQ GQFGGRPHPT ILAAAALLGV DEVWAVGGAQ
210 220 230 240 250
AVALLAYGGT DTDGAELAPV DMITGPGNIY VTAAKRICRS QVGIDAEAGP
260 270 280 290 300
TEIAILADHT ADPVHVAADL ISQAEHDEMA ASVLVTDSET LAEATDRELA
310 320 330 340 350
NQLATTKHVE RVTAALSGKQ SAIVLVDDID AGVRTVNAYA AEHLEIQTVD
360 370 380 390 400
APGVAGRIRS AGAIFVGAWS PVSLGDYCAG SNHVLPTAGC ARHSSGLSVQ
410 420 430 440
TFLRGIHVVE YDEAALKDVS GHVITLSKAE DLPAHGEAVR RRFER
Length:445
Mass (Da):46,703
Last modified:December 1, 1992 - v1
Checksum:i19996D28D4591170
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65542 Genomic DNA. Translation: CAA46509.1.
PIRiS26209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65542 Genomic DNA. Translation: CAA46509.1.
PIRiS26209.

3D structure databases

ProteinModelPortaliP28736.
SMRiP28736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_3205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.

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_MYCSM
AccessioniPrimary (citable) accession number: P28736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
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

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.