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Reviewed, UniProtKB/Swiss-Prot P39071 (DHBA_BACSU)

Last modified November 25, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
    EC=1.3.1.28
Alternative name(s):
    Cold shock protein CSI14
Gene names
Name: dhbA
Synonyms: entA
Ordered Locus Names: BSU32000
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) = 2,3-dihydroxybenzoate + NADH.

Pathway

Siderophore biosynthesis; bacillibactin biosynthesis.

Subcellular location

Cytoplasm.

Induction

In response to low temperature.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords

   Biological processStress response
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processenterobactin biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2612612,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
PRO_0000054601

Regions

Nucleotide binding12 – 3625NAD By similarity

Sites

Active site1571Proton acceptor By similarity
Binding site1441Substrate By similarity

Experimental info

Sequence conflict1461P → D in AAA16899. Ref.3
Sequence conflict231 – 2344IADA → MRC in AAA16899. Ref.3
Sequence conflict247 – 25610TMHNLCVDGG → RCIFMRRCAT Ref.3

Sequences

Sequence LengthMass (Da)Tools
P39071-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 00B0EFBA53AB407C

FASTA26127,494
        10         20         30         40         50         60 
MNAKGIEGKI AFITGAAQGI GEAVARTLAS QGAHIAAVDY NPEKLEKVVS SLKAEARHAE 

        70         80         90        100        110        120 
AFPADVRDSA AIDEITARIE REMGPIDILV NVAGVLRPGL IHSLSDEEWE ATFSVNSTGV 

       130        140        150        160        170        180 
FNASRSVSKY MMDRRSGSIV TVGSNPAGVP RTSMAAYASS KAAAVMFTKC LGLELAEYNI 

       190        200        210        220        230        240 
RCNIVSPGST ETDMQWSLWA DENGAEQVIK GSLETFKTGI PLKKLAKPSD IADAVLFLVS 

       250        260 
GQAGHITMHN LCVDGGATLG V 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes."
Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W.
Gene 178:119-123(1996) [PubMed: 8921902] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg.
[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.
[3]"Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes."
Adams R., Schumann W.
Gene 133:119-121(1993) [PubMed: 8224884] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-256.
Strain: 168.
[4]Graumann P.L., Schmid R., Marahiel M.A.
Submitted (OCT-1997) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-11.
Strain: 168 / JH642.

Cross-references

Sequence databases

U26444 Genomic DNA. Translation: AAC44630.1.
Z99120 Genomic DNA. Translation: CAB15190.1.
L08644 Genomic DNA. Translation: AAA16899.2.
PIRA69615.
RefSeqNP_391080.1.

3D structure databases

HSSPHSSP built from PDB template 1CYD based on UniProtKB P08074.
ModBaseSearch...

Genome annotation databases

GeneID936579.
GenomeReviewsGene locus BSU32000 in contig AL009126_GR.
KEGGbsu:BSU32000.
NMPDRfig|224308.1.peg.3206.

Organism-specific databases

SubtiListBG11019. dhbA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP39071.

Enzyme and pathway databases

BioCycBSUB224308:BSU3197-MON.
MetaCyc:MON-13913.

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
IPR003560. DHB_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR01397. DHBDHDRGNASE.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHBA_BACSU
AccessionPrimary (citable) accession number: P39071
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents