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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (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)DescriptionActionsGraphical viewLength
Binding sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi361ZincUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei415SubstrateUniRule annotation1
Metal bindingi420ZincUniRule annotation1
Binding sitei420SubstrateUniRule 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

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:NMA1770
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000626 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358011 – 429Histidinol dehydrogenaseAdd BLAST429

Structurei

3D structure databases

ProteinModelPortaliQ9JTH9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

Q9JTH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE
60 70 80 90 100
YTNKFDQTNA KSIDDLILTQ ADLKAAFERI PNDVQTALQT AARRVESYHQ
110 120 130 140 150
RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH
160 170 180 190 200
VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAVAALAYGT
210 220 230 240 250
ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD
260 270 280 290 300
WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA
310 320 330 340 350
SLGNRGAMIL AKDLDEACEI ANYISPEHLE LSVENPQEWA KKIRHAGAIF
360 370 380 390 400
MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG
410 420
AQKLGETASV LAHGESLTAH ARAAEFRMK
Length:429
Mass (Da):46,338
Last modified:October 1, 2000 - v1
Checksum:iE45EAF3C5B0F1E32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM08897.1.
PIRiB81802.
RefSeqiWP_002216785.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM08897; CAM08897; NMA1770.
KEGGinma:NMA1770.
PATRICi20364836. VBINeiMen132687_2120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM08897.1.
PIRiB81802.
RefSeqiWP_002216785.1. NC_003116.1.

3D structure databases

ProteinModelPortaliQ9JTH9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM08897; CAM08897; NMA1770.
KEGGinma:NMA1770.
PATRICi20364836. VBINeiMen132687_2120.

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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_NEIMA
AccessioniPrimary (citable) accession number: Q9JTH9
Secondary accession number(s): A1ISY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 99 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

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.