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Q8DTQ7 (HISX_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:SMU_1270
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135858

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2551Zinc By similarity
Metal binding2581Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1271NAD By similarity
Binding site1871NAD By similarity
Binding site2101NAD By similarity
Binding site2331Substrate By similarity
Binding site2551Substrate By similarity
Binding site2581Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DTQ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F84C6A4E72E08EF2

FASTA42746,451
        10         20         30         40         50         60 
MKRLTGTNEK ISNILYQEQL ELSKENLDVE ATVREIIEKV KEEGDEALRA YSEKFDHVVL 

        70         80         90        100        110        120 
SELHVSDQVV NEAFDKIDKD VLTALENAKA NIESYHKQQL KGGFEDQPSQ GVLRGQLIRP 

       130        140        150        160        170        180 
IERVGVYVPG GTAAYPSSVL MNVIPAKIAG VKEIIMITPP QEHFVPAILV AAKLAGVDKI 

       190        200        210        220        230        240 
YQVGGAQGIA ALAYGTQTLP KVDKITGPGN IFVATAKKLV YGVVGIDMIA GPSEIGVIAD 

       250        260        270        280        290        300 
STANPVYVAA DLLSQAEHDV HARAILVTNS AELADAVELE IEKQLQTLPR QAIARPSIEN 

       310        320        330        340        350        360 
NGRIIIAQDV ESMFELMNLV APEHLEIAID KAYDYLERVQ NAGSIFLGHY TSEPIGDYYA 

       370        380        390        400        410        420 
GANHVLPTTA TSRFSSALGV HDFVKRIQYT QYSKAAVNAA EKDITTLAYA EGLQAHARAI 


EVRNDKN 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58952.1.
RefSeqNP_721646.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DTQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58952; AAN58952; SMU_1270.
GeneID1028553.
KEGGsmu:SMU_1270.
PATRIC19664619. VBIStrMut61772_1139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAICGPGNK.
OrthoDBEOG6CVVCR.
PhylomeDBQ8DTQ7.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-1205-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_STRMU
AccessionPrimary (citable) accession number: Q8DTQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways