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Q46WL2

- HISX_CUPPJ

UniProt

Q46WL2 - HISX_CUPPJ

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
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 sitei144 – 1441NADUniRule annotation
Binding sitei205 – 2051NADUniRule annotation
Binding sitei228 – 2281NADUniRule annotation
Binding sitei251 – 2511SubstrateUniRule annotation
Metal bindingi273 – 2731ZincUniRule annotation
Binding sitei273 – 2731SubstrateUniRule annotation
Metal bindingi276 – 2761ZincUniRule annotation
Binding sitei276 – 2761SubstrateUniRule annotation
Active sitei341 – 3411Proton acceptorUniRule annotation
Active sitei342 – 3421Proton acceptorUniRule annotation
Binding sitei342 – 3421SubstrateUniRule annotation
Metal bindingi375 – 3751ZincUniRule annotation
Binding sitei375 – 3751SubstrateUniRule annotation
Binding sitei429 – 4291SubstrateUniRule annotation
Metal bindingi434 – 4341ZincUniRule annotation
Binding sitei434 – 4341SubstrateUniRule 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

BioCyciCPIN264198:GIW3-3165-MONOMER.
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:Reut_A3111
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002697: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Histidinol dehydrogenasePRO_0000135826Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_A3111.

Structurei

3D structure databases

ProteinModelPortaliQ46WL2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
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.

Q46WL2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNATEMENVS IRRLDSSDPR FAQALREVLA FEAGEDEAID RAVAQILADV
60 70 80 90 100
KDRGDAAVLE YTQRFDRVEA ASMGALEISQ SELEAALEDL EPKRRAALEA
110 120 130 140 150
AAARVRAYHE KQKIECGSHS WEYTEADGTM LGQKVTPLDR VGIYVPGGKA
160 170 180 190 200
AYPSSVLMNA IPARVAGVKE IIMVVPTPGG VRNELVLAAA QIAGVDRVFT
210 220 230 240 250
IGGAQAVGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG TVGIDMIAGP
260 270 280 290 300
SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAD YIAQVEASIQ
310 320 330 340 350
RQLDSMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP
360 370 380 390 400
RQWSEKIRHA GAIFLGRYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD
410 420 430 440
FQKRSSLIEV SEGGAQMLGQ IAAELAYGEG LQAHARSAEY RFKRS
Length:445
Mass (Da):47,888
Last modified:September 13, 2005 - v1
Checksum:i4E3DF54A378ADE4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62471.1.
RefSeqiWP_011299254.1. NC_007347.1.
YP_297315.1. NC_007347.1.

Genome annotation databases

EnsemblBacteriaiAAZ62471; AAZ62471; Reut_A3111.
GeneIDi3611937.
KEGGireu:Reut_A3111.
PATRICi20231936. VBIRalEut24049_3794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62471.1 .
RefSeqi WP_011299254.1. NC_007347.1.
YP_297315.1. NC_007347.1.

3D structure databases

ProteinModelPortali Q46WL2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264198.Reut_A3111.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ62471 ; AAZ62471 ; Reut_A3111 .
GeneIDi 3611937.
KEGGi reu:Reut_A3111.
PATRICi 20231936. VBIRalEut24049_3794.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci CPIN264198:GIW3-3165-MONOMER.

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. "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JMP134 / LMG 1197.

Entry informationi

Entry nameiHISX_CUPPJ
AccessioniPrimary (citable) accession number: Q46WL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: November 26, 2014
This is version 67 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

External Data

Dasty 3