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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
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. no protein annotated in this organism
  3. Phosphoribosyl-AMP cyclohydrolase (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. 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 sitei127NADUniRule annotation1
Binding sitei187NADUniRule annotation1
Binding sitei210NADUniRule annotation1
Binding sitei233SubstrateUniRule annotation1
Metal bindingi255ZincUniRule annotation1
Binding sitei255SubstrateUniRule annotation1
Metal bindingi258ZincUniRule annotation1
Binding sitei258SubstrateUniRule annotation1
Active sitei323Proton acceptorUniRule annotation1
Active sitei324Proton acceptorUniRule annotation1
Binding sitei324SubstrateUniRule annotation1
Metal bindingi357ZincUniRule annotation1
Binding sitei357SubstrateUniRule annotation1
Binding sitei411SubstrateUniRule annotation1
Metal bindingi416ZincUniRule annotation1
Binding sitei416SubstrateUniRule 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:SMU_1270
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358581 – 427Histidinol dehydrogenaseAdd BLAST427

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_1270.

Structurei

3D structure databases

ProteinModelPortaliQ8DTQ7.
SMRiQ8DTQ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiGGTARFY.
PhylomeDBiQ8DTQ7.

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.

Q8DTQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRLTGTNEK ISNILYQEQL ELSKENLDVE ATVREIIEKV KEEGDEALRA
60 70 80 90 100
YSEKFDHVVL SELHVSDQVV NEAFDKIDKD VLTALENAKA NIESYHKQQL
110 120 130 140 150
KGGFEDQPSQ GVLRGQLIRP IERVGVYVPG GTAAYPSSVL MNVIPAKIAG
160 170 180 190 200
VKEIIMITPP QEHFVPAILV AAKLAGVDKI YQVGGAQGIA ALAYGTQTLP
210 220 230 240 250
KVDKITGPGN IFVATAKKLV YGVVGIDMIA GPSEIGVIAD STANPVYVAA
260 270 280 290 300
DLLSQAEHDV HARAILVTNS AELADAVELE IEKQLQTLPR QAIARPSIEN
310 320 330 340 350
NGRIIIAQDV ESMFELMNLV APEHLEIAID KAYDYLERVQ NAGSIFLGHY
360 370 380 390 400
TSEPIGDYYA GANHVLPTTA TSRFSSALGV HDFVKRIQYT QYSKAAVNAA
410 420
EKDITTLAYA EGLQAHARAI EVRNDKN
Length:427
Mass (Da):46,451
Last modified:March 1, 2003 - v1
Checksum:iF84C6A4E72E08EF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58952.1.
RefSeqiNP_721646.1. NC_004350.2.
WP_002263174.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58952; AAN58952; SMU_1270.
GeneIDi1028553.
KEGGismu:SMU_1270.
PATRICi19664619. VBIStrMut61772_1139.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58952.1.
RefSeqiNP_721646.1. NC_004350.2.
WP_002263174.1. NC_004350.2.

3D structure databases

ProteinModelPortaliQ8DTQ7.
SMRiQ8DTQ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_1270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58952; AAN58952; SMU_1270.
GeneIDi1028553.
KEGGismu:SMU_1270.
PATRICi19664619. VBIStrMut61772_1139.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiGGTARFY.
PhylomeDBiQ8DTQ7.

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_STRMU
AccessioniPrimary (citable) accession number: Q8DTQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
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, 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.