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Q8FNZ0

- HISX_COREF

UniProt

Q8FNZ0 - HISX_COREF

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291NADUniRule annotation
Binding sitei193 – 1931NADUniRule annotation
Binding sitei218 – 2181NADUniRule annotation
Binding sitei241 – 2411SubstrateUniRule annotation
Metal bindingi263 – 2631ZincUniRule annotation
Binding sitei263 – 2631SubstrateUniRule annotation
Metal bindingi266 – 2661ZincUniRule annotation
Binding sitei266 – 2661SubstrateUniRule annotation
Active sitei332 – 3321Proton acceptorUniRule annotation
Active sitei333 – 3331Proton acceptorUniRule annotation
Binding sitei333 – 3331SubstrateUniRule annotation
Metal bindingi366 – 3661ZincUniRule annotation
Binding sitei366 – 3661SubstrateUniRule annotation
Binding sitei420 – 4201SubstrateUniRule annotation
Metal bindingi425 – 4251ZincUniRule annotation
Binding sitei425 – 4251SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
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:CE2003
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Histidinol dehydrogenasePRO_0000135760Add
BLAST

Proteomic databases

PRIDEiQ8FNZ0.

Interactioni

Protein-protein interaction databases

STRINGi196164.CE2003.

Structurei

3D structure databases

ProteinModelPortaliQ8FNZ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiDEMAMPI.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
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.

Q8FNZ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNVTDLRGH TPSKSDIRRA LPRGGTDVVS VLPIVEPVVD DVQNRGAEAA
60 70 80 90 100
LDYGEKFDHI RPASVRVPAE VLKAAEDTLD PRVREAIEES IRRVRKVHAD
110 120 130 140 150
QKPREHTTEL APGGTVTERF LPIDRVGLYV PGGNAVYPSS VIMNAVPAQE
160 170 180 190 200
AGVGTLVVAS PPQADHGGWP HPTILAACSI LGVDEVWAVG GAQAVALLAF
210 220 230 240 250
GDDSADLEPV DIITGPGNIF VTAAKRLVRG VVGTDSEAGP TEIAILADDT
260 270 280 290 300
ANPVNVAYDL ISQAEHDVMA ASVLITDSEQ LARDVNREIE ARYAITRNAD
310 320 330 340 350
RVAEALRGKQ SGIVLVDDIE VGIAVADQYA AEHLEVHTAN AREVSERISN
360 370 380 390 400
AGAIFVGDFS PVPLGDYSAG SNHVLPTSGT ARFSAGLSTH TFLRPVNLIE
410 420 430 440 450
YDEAALKDIS EVVINFADAE DLPAHGEAIR ARFETLPTTT ADTTDTPDAT

A
Length:451
Mass (Da):47,770
Last modified:March 1, 2003 - v1
Checksum:i5A2D5AA7B990ECCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18813.1.
RefSeqiNP_738613.1. NC_004369.1.
WP_006768001.1. NZ_GG700683.1.

Genome annotation databases

EnsemblBacteriaiBAC18813; BAC18813; BAC18813.
GeneIDi1032060.
KEGGicef:CE2003.
PATRICi21490139. VBICorEff9312_1984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18813.1 .
RefSeqi NP_738613.1. NC_004369.1.
WP_006768001.1. NZ_GG700683.1.

3D structure databases

ProteinModelPortali Q8FNZ0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE2003.

Proteomic databases

PRIDEi Q8FNZ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC18813 ; BAC18813 ; BAC18813 .
GeneIDi 1032060.
KEGGi cef:CE2003.
PATRICi 21490139. VBICorEff9312_1984.

Phylogenomic databases

HOGENOMi HOG000243914.
KOi K00013.
OMAi DEMAMPI.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiHISX_COREF
AccessioniPrimary (citable) accession number: Q8FNZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 86 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

External Data

Dasty 3