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O34651

- HISX_BACSU

UniProt

O34651 - HISX_BACSU

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus subtilis (strain 168)
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.By similarity

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231NADBy similarity
Binding sitei185 – 1851NADBy similarity
Binding sitei208 – 2081NADBy similarity
Binding sitei231 – 2311SubstrateBy similarity
Metal bindingi253 – 2531ZincBy similarity
Binding sitei253 – 2531SubstrateBy similarity
Metal bindingi256 – 2561ZincBy similarity
Binding sitei256 – 2561SubstrateBy similarity
Active sitei321 – 3211Proton acceptorBy similarity
Active sitei322 – 3221Proton acceptorBy similarity
Binding sitei322 – 3221SubstrateBy similarity
Metal bindingi355 – 3551ZincBy similarity
Binding sitei355 – 3551SubstrateBy similarity
Binding sitei409 – 4091SubstrateBy similarity
Metal bindingi414 – 4141ZincBy similarity
Binding sitei414 – 4141SubstrateBy similarity

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

BioCyciBSUB:BSU34910-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
Ordered Locus Names:BSU34910
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU34910. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Histidinol dehydrogenasePRO_0000135728Add
BLAST

Proteomic databases

PaxDbiO34651.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU34910.

Structurei

3D structure databases

ProteinModelPortaliO34651.
SMRiO34651. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiO34651.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.
PhylomeDBiO34651.

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.

O34651-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK
60 70 80 90 100
FDCIEIDSPL VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW
110 120 130 140 150
FYHRKDGTML GQKVTALDSA GVYVPGGTAA YPSSVLMNVI PALVAGVERI
160 170 180 190 200
VLVTPPGKDG LLSPGVLVAA AELGIKDIYK MGGAQAIAAL AYGTETIEPV
210 220 230 240 250
DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET AIPSEIAADL
260 270 280 290 300
LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG
310 320 330 340 350
CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP
360 370 380 390 400
EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE
410 420
SIAAFARLEG LEAHARSIEA RERRISK
Length:427
Mass (Da):46,256
Last modified:January 1, 1998 - v1
Checksum:iBDB0B2AE3C580E7F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017113 Genomic DNA. Translation: AAC67295.1.
AL009126 Genomic DNA. Translation: CAB15496.1.
PIRiA69641.
RefSeqiNP_391371.1. NC_000964.3.
WP_003243286.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB15496; CAB15496; BSU34910.
GeneIDi936584.
KEGGibsu:BSU34910.
PATRICi18978988. VBIBacSub10457_3656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017113 Genomic DNA. Translation: AAC67295.1 .
AL009126 Genomic DNA. Translation: CAB15496.1 .
PIRi A69641.
RefSeqi NP_391371.1. NC_000964.3.
WP_003243286.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali O34651.
SMRi O34651. Positions 2-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU34910.

Proteomic databases

PaxDbi O34651.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15496 ; CAB15496 ; BSU34910 .
GeneIDi 936584.
KEGGi bsu:BSU34910.
PATRICi 18978988. VBIBacSub10457_3656.

Organism-specific databases

GenoListi BSU34910. [Micado ]

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
InParanoidi O34651.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.
PhylomeDBi O34651.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci BSUB:BSU34910-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

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiHISX_BACSU
AccessioniPrimary (citable) accession number: O34651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 108 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3