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Q5QWP8

- HISX_IDILO

UniProt

Q5QWP8 - HISX_IDILO

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
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 sitei132 – 1321NADUniRule annotation
Binding sitei194 – 1941NADUniRule annotation
Binding sitei217 – 2171NADUniRule annotation
Binding sitei243 – 2431SubstrateUniRule annotation
Metal bindingi265 – 2651ZincUniRule annotation
Binding sitei265 – 2651SubstrateUniRule annotation
Metal bindingi268 – 2681ZincUniRule annotation
Binding sitei268 – 2681SubstrateUniRule 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

BioCyciILOI283942:GI0U-1845-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:IL1835
OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Taxonomic identifieri283942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
ProteomesiUP000001171: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Histidinol dehydrogenasePRO_0000135781Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi283942.IL1835.

Structurei

3D structure databases

ProteinModelPortaliQ5QWP8.
SMRiQ5QWP8. Positions 7-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
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.

Q5QWP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSELRIPIEQ WQSLSSAEQT QRLARPGRAQ AESLREKVAV ILSDVRDNGE
60 70 80 90 100
RAVLNYTRQF DNPDATSLRM SDEQVEAAVA SLDDKVKRAI DTAYQTIYRF
110 120 130 140 150
HEAQRPQDLS IETAPGVQCE LRYAPLDAVG LYIPGGSATL PSTALMLGVP
160 170 180 190 200
AQIAGCQRVV MVSPPNKQGE LPAALLYAAK RCGVTDILLC GGAQAIGALA
210 220 230 240 250
YGIESSPAVG KVFGPGNSFV TEAKQQVSQN DSGCAMDLPA GPSELLVIAD
260 270 280 290 300
DSANPAYVAA DLLSQAEHGP DSQVILLTPS MTVAENVRQE LMAQCAQLSR
310 320 330 340 350
ADIAEQALQA SRLLVVADMN EAIAISETYA PEHLSIQTDN ARDLLPQLTR
360 370 380 390 400
AGSVFVGHYT PESGGDYATG TNHVLPTYGY ARNYSSLGLV DFYRRYTVQE
410 420 430 440
ASHDGLRQLA EAITTLADVE GLDAHKRAVT IRTETKSTES KL
Length:442
Mass (Da):47,447
Last modified:January 4, 2005 - v1
Checksum:i45D9665DC7D9465F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV82667.1.
RefSeqiYP_156216.1. NC_006512.1.

Genome annotation databases

EnsemblBacteriaiAAV82667; AAV82667; IL1835.
GeneIDi3173855.
KEGGiilo:IL1835.
PATRICi22141786. VBIIdiLoi21852_1842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV82667.1 .
RefSeqi YP_156216.1. NC_006512.1.

3D structure databases

ProteinModelPortali Q5QWP8.
SMRi Q5QWP8. Positions 7-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 283942.IL1835.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV82667 ; AAV82667 ; IL1835 .
GeneIDi 3173855.
KEGGi ilo:IL1835.
PATRICi 22141786. VBIIdiLoi21852_1842.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci ILOI283942:GI0U-1845-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Entry informationi

Entry nameiHISX_IDILO
AccessioniPrimary (citable) accession number: Q5QWP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: November 26, 2014
This is version 74 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