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O34651 (HISX_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:BSU34910
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Histidinol dehydrogenase HAMAP MF_01024
PRO_0000135728

Sites

Active site3211Proton acceptor By similarity
Active site3221Proton acceptor By similarity
Metal binding2531Zinc By similarity
Metal binding2561Zinc By similarity
Metal binding3551Zinc By similarity
Metal binding4141Zinc By similarity
Binding site1231NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2311Substrate By similarity
Binding site2531Substrate By similarity
Binding site2561Substrate By similarity
Binding site3221Substrate By similarity
Binding site3551Substrate By similarity
Binding site4091Substrate By similarity
Binding site4141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O34651 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BDB0B2AE3C580E7F

FASTA42746,256
        10         20         30         40         50         60 
MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK FDCIEIDSPL 

        70         80         90        100        110        120 
VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW FYHRKDGTML GQKVTALDSA 

       130        140        150        160        170        180 
GVYVPGGTAA YPSSVLMNVI PALVAGVERI VLVTPPGKDG LLSPGVLVAA AELGIKDIYK 

       190        200        210        220        230        240 
MGGAQAIAAL AYGTETIEPV DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET 

       250        260        270        280        290        300 
AIPSEIAADL LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG 

       310        320        330        340        350        360 
CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP EPVGDYFAGP 

       370        380        390        400        410        420 
NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE SIAAFARLEG LEAHARSIEA 


RERRISK

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis."
Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF017113 Genomic DNA. Translation: AAC67295.1.
AL009126 Genomic DNA. Translation: CAB15496.1.
PIRA69641.
RefSeqNP_391371.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34651.
SMRO34651. Positions 2-427.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002743; EBBACP00000002743; EBBACG00000002738.
GeneID936584.
GenomeReviewsGene locus BSU34910 in contig AL009126_GR.
KEGGbsu:BSU34910.
NMPDRfig|224308.1.peg.3497.
PATRIC18978988. VBIBacSub10457_3656.

Organism-specific databases

GenoListBSU34910. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002843.
HOGENOMHBG329596.
OMANRYVTEA.
PhylomeDBO34651.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBSUB:BSU34910-MONOMER.

Family and domain databases

HAMAPMF_01024. HisD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
KOK00013.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. HisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BACSU
AccessionPrimary (citable) accession number: O34651
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents