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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Reviewed-Annotation score: 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
ProteomesiUP000000608 Componenti: Chromosome UP000000606 Componenti: 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.
OMAiLSVQSFL.
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.
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.
RefSeqiYP_006715017.1. NC_006322.1.
YP_080822.1. NC_006270.3.

3D structure databases

ProteinModelPortaliQ65EF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BL03408.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciBLIC279010:GJ2P-3694-MONOMER.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.