DHBB_BACSU
ID DHBB_BACSU Reviewed; 312 AA.
AC P45743;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Isochorismatase;
DE EC=3.3.2.1;
DE AltName: Full=2,3 dihydro-2,3 dihydroxybenzoate synthase;
DE AltName: Full=Superoxide-inducible protein 1;
DE Short=SOI1;
GN Name=dhbB; OrderedLocusNames=BSU31970;
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=8550523; DOI=10.1128/jb.178.3.854-861.1996;
RA Rowland B.M., Taber H.W.;
RT "Duplicate isochorismate synthase genes of Bacillus subtilis: regulation
RT and involvement in the biosyntheses of menaquinone and 2,3-
RT dihydroxybenzoate.";
RL J. Bacteriol. 178:854-861(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 PROTEIN SEQUENCE OF 1-16.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-
CC dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1;
CC -!- PATHWAY: Siderophore biosynthesis; bacillibactin biosynthesis.
CC -!- INDUCTION: By superoxide.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; U26444; AAC44633.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15187.1; -; Genomic_DNA.
DR PIR; B69615; B69615.
DR RefSeq; NP_391077.1; NC_000964.3.
DR RefSeq; WP_003228749.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P45743; -.
DR SMR; P45743; -.
DR IntAct; P45743; 2.
DR MINT; P45743; -.
DR STRING; 224308.BSU31970; -.
DR jPOST; P45743; -.
DR PaxDb; P45743; -.
DR PRIDE; P45743; -.
DR EnsemblBacteria; CAB15187; CAB15187; BSU_31970.
DR GeneID; 936582; -.
DR KEGG; bsu:BSU31970; -.
DR PATRIC; fig|224308.179.peg.3463; -.
DR eggNOG; COG1535; Bacteria.
DR eggNOG; COG3433; Bacteria.
DR InParanoid; P45743; -.
DR OMA; RDIKPFF; -.
DR PhylomeDB; P45743; -.
DR BioCyc; BSUB:BSU31970-MON; -.
DR BioCyc; MetaCyc:MON-13911; -.
DR UniPathway; UPA00013; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008908; F:isochorismatase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016291; Isochorismatase.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00857; Isochorismatase; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001111; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Isochorismatase"
FT /id="PRO_0000201821"
FT DOMAIN 229..302
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 263
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 312 AA; 35107 MW; 3A737A4C7BC53DDC CRC64;
MAIPAIQPYQ MPTASDMPQN KVSWVPDPNR AVLLIHDMQN YFVDAFTAGA SPVTELSANI
RKLKNQCVQL GIPVVYTAQP GSQNPDDRAL LTDFWGPGLN SGPYEEKIIT ELAPEDDDLV
LTKWRYSAFK RTNLLEMMRK EGRDQLIITG IYAHIGCLVT ACEAFMEDIK AFFVGDAVAD
FSLEKHQMAL EYAAGRCAFT VMTDSLLDQL QNAPADVQKT SANTGKKNVF TCENIRKQIA
ELLQETPEDI TDQEDLLDRG LDSVRIMTLV EQWRREGAEV TFVELAERPT IEEWQKLLTT
RSQQVLPNAD YL
