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Q65EF9

- HISX_BACLD

UniProt

Q65EF9 - HISX_BACLD

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
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 sitei123 – 1231NADUniRule annotation
Binding sitei185 – 1851NADUniRule annotation
Binding sitei208 – 2081NADUniRule annotation
Binding sitei231 – 2311SubstrateUniRule annotation
Metal bindingi253 – 2531ZincUniRule annotation
Binding sitei253 – 2531SubstrateUniRule annotation
Metal bindingi256 – 2561ZincUniRule annotation
Binding sitei256 – 2561SubstrateUniRule annotation
Active sitei321 – 3211Proton acceptorUniRule annotation
Active sitei322 – 3221Proton acceptorUniRule annotation
Binding sitei322 – 3221SubstrateUniRule annotation
Metal bindingi355 – 3551ZincUniRule annotation
Binding sitei355 – 3551SubstrateUniRule annotation
Binding sitei409 – 4091SubstrateUniRule annotation
Metal bindingi414 – 4141ZincUniRule annotation
Binding sitei414 – 4141SubstrateUniRule 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

BioCyciBLIC279010:GJ2P-3694-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:BLi03736, BL03408
OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)
Taxonomic identifieri279010 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000000606: Chromosome, UP000000608: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Histidinol dehydrogenasePRO_0000135727Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi279010.BL03408.

Structurei

3D structure databases

ProteinModelPortaliQ65EF9.
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.

Q65EF9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKSISGNT SVSLKRSIDA GTEEQRKAVR GIIEEVKKNG NAAVSAFTRQ
60 70 80 90 100
FDGADVAGFR VSEEEIKEAY SALEERDLEI IQAAIFNIKE YHERQLATSW
110 120 130 140 150
FYHRKDGTML GQKITPLDSA GVYVPGGTAA YPSSVLMNVI PALVAGVDRI
160 170 180 190 200
VLASPPGKDG KLSAGVLAAA AELGVTEIYK MGGAQAIAAL AYGTETITPV
210 220 230 240 250
DKITGPGNIY VALAKREVFG QVDIDMIAGP SEIAILADST ANYREIAADL
260 270 280 290 300
LSQAEHDAMA SSILVTDSET LAESVLKEVY RQLEHLPRKE IARQSIDNYG
310 320 330 340 350
LIYVTETMNE AVSVINELAP EHLEILTVQP DALLGQIKHA GAIFLGRYSS
360 370 380 390 400
EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKRSSIISY SREAFRANAE
410 420
KIAAFARLEG LEAHARAIES RNREED
Length:426
Mass (Da):46,028
Last modified:October 25, 2004 - v1
Checksum:i76A087539E215CA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU42555.1.
CP000002 Genomic DNA. Translation: AAU25184.1.
RefSeqiYP_006715017.1. NC_006322.1.
YP_080822.1. NC_006270.3.

Genome annotation databases

EnsemblBacteriaiAAU25184; AAU25184; BL03408.
AAU42555; AAU42555; BLi03736.
GeneIDi3027872.
3100933.
KEGGibld:BLi03736.
bli:BL03408.
PATRICi18953260. VBIBacLic203714_3805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU42555.1 .
CP000002 Genomic DNA. Translation: AAU25184.1 .
RefSeqi YP_006715017.1. NC_006322.1.
YP_080822.1. NC_006270.3.

3D structure databases

ProteinModelPortali Q65EF9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279010.BL03408.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU25184 ; AAU25184 ; BL03408 .
AAU42555 ; AAU42555 ; BLi03736 .
GeneIDi 3027872.
3100933.
KEGGi bld:BLi03736.
bli:BL03408.
PATRICi 18953260. VBIBacLic203714_3805.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci BLIC279010:GJ2P-3694-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. "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
    Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.

Entry informationi

Entry nameiHISX_BACLD
AccessioniPrimary (citable) accession number: Q65EF9
Secondary accession number(s): Q62PX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 25, 2004
Last modified: November 26, 2014
This is version 79 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