DHBA_BACSU
ID DHBA_BACSU Reviewed; 261 AA.
AC P39071;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase;
DE EC=1.3.1.28;
DE AltName: Full=Cold shock protein CSI14;
GN Name=dhbA; Synonyms=entA; OrderedLocusNames=BSU32000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8921902; DOI=10.1016/0378-1119(96)00349-6;
RA Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W.;
RT "Sequence and genetic organization of a Bacillus subtilis operon encoding
RT 2,3-dihydroxybenzoate biosynthetic enzymes.";
RL Gene 178:119-123(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 56 AND 146.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-256.
RC STRAIN=168;
RX PubMed=8224884; DOI=10.1016/0378-1119(93)90235-u;
RA Adams R., Schumann W.;
RT "Cloning and mapping of the Bacillus subtilis locus homologous to
RT Escherichia coli ent genes.";
RL Gene 133:119-121(1993).
RN [5]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=168 / JH642;
RA Graumann P.L., Schmid R., Marahiel M.A.;
RL Submitted (OCT-1997) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-
CC dihydroxybenzoate + H(+) + NADH; Xref=Rhea:RHEA:23824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36654, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58764; EC=1.3.1.28;
CC -!- PATHWAY: Siderophore biosynthesis; bacillibactin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: In response to low temperature.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U26444; AAC44630.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15190.2; -; Genomic_DNA.
DR EMBL; L08644; AAA16899.2; -; Genomic_DNA.
DR PIR; A69615; A69615.
DR RefSeq; NP_391080.2; NC_000964.3.
DR RefSeq; WP_003244476.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P39071; -.
DR SMR; P39071; -.
DR IntAct; P39071; 1.
DR MINT; P39071; -.
DR STRING; 224308.BSU32000; -.
DR jPOST; P39071; -.
DR PaxDb; P39071; -.
DR PRIDE; P39071; -.
DR EnsemblBacteria; CAB15190; CAB15190; BSU_32000.
DR GeneID; 936579; -.
DR KEGG; bsu:BSU32000; -.
DR PATRIC; fig|224308.179.peg.3466; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P39071; -.
DR OMA; AKDANTM; -.
DR PhylomeDB; P39071; -.
DR BioCyc; BSUB:BSU32000-MON; -.
DR BioCyc; MetaCyc:MON-13913; -.
DR UniPathway; UPA00013; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008667; F:2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0071281; P:cellular response to iron ion; IDA:CollecTF.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR CDD; cd05331; DH-DHB-DH_SDR_c; 1.
DR InterPro; IPR003560; DHB_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR01397; DHBDHDRGNASE.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR04316; dhbA_paeA; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome; Stress response.
FT CHAIN 1..261
FT /note="2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase"
FT /id="PRO_0000054601"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 12..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 56
FT /note="G -> A (in Ref. 1; AAC44630)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> D (in Ref. 4; AAA16899)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> P (in Ref. 1; AAC44630)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..234
FT /note="IADA -> MRC (in Ref. 4; AAA16899)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..256
FT /note="TMHNLCVDGG -> RCIFMRRC (in Ref. 4; AAA16899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 27454 MW; 9D85362BC1B5F9AC CRC64;
MNAKGIEGKI AFITGAAQGI GEAVARTLAS QGAHIAAVDY NPEKLEKVVS SLKAEGRHAE
AFPADVRDSA AIDEITARIE REMGPIDILV NVAGVLRPGL IHSLSDEEWE ATFSVNSTGV
FNASRSVSKY MMDRRSGSIV TVGSNAAGVP RTSMAAYASS KAAAVMFTKC LGLELAEYNI
RCNIVSPGST ETDMQWSLWA DENGAEQVIK GSLETFKTGI PLKKLAKPSD IADAVLFLVS
GQAGHITMHN LCVDGGATLG V
