DHBC_BACSU
ID DHBC_BACSU Reviewed; 398 AA.
AC P45744;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Isochorismate synthase DhbC;
DE EC=5.4.4.2;
DE AltName: Full=Isochorismate mutase;
GN Name=dhbC; OrderedLocusNames=BSU31990;
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 SEQUENCE REVISION TO 239.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC -!- PATHWAY: Siderophore biosynthesis; bacillibactin biosynthesis.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000305}.
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DR EMBL; U26444; AAC44631.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15189.2; -; Genomic_DNA.
DR PIR; C69615; C69615.
DR RefSeq; NP_391079.2; NC_000964.3.
DR RefSeq; WP_003243699.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P45744; -.
DR SMR; P45744; -.
DR IntAct; P45744; 1.
DR MINT; P45744; -.
DR STRING; 224308.BSU31990; -.
DR iPTMnet; P45744; -.
DR PaxDb; P45744; -.
DR PRIDE; P45744; -.
DR EnsemblBacteria; CAB15189; CAB15189; BSU_31990.
DR GeneID; 937162; -.
DR KEGG; bsu:BSU31990; -.
DR PATRIC; fig|224308.179.peg.3465; -.
DR eggNOG; COG1169; Bacteria.
DR InParanoid; P45744; -.
DR OMA; TMWHLSS; -.
DR PhylomeDB; P45744; -.
DR BioCyc; BSUB:BSU31990-MON; -.
DR BioCyc; MetaCyc:MON-13807; -.
DR UniPathway; UPA00013; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008909; F:isochorismate synthase activity; IBA:GO_Central.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR004561; IsoChor_synthase.
DR Pfam; PF00425; Chorismate_bind; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00543; isochor_syn; 1.
PE 1: Evidence at protein level;
KW Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..398
FT /note="Isochorismate synthase DhbC"
FT /id="PRO_0000154146"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 239
FT /note="S -> P (in Ref. 1; AAC44631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43436 MW; 22F30D14817E8492 CRC64;
MLDQNVITET KAEHLLHEYQ PGAFFLASPH RVLLAKGICE IVPEADGQNQ METLSGRIAE
ALRQAKQSGQ SRPLVVGAVP FDQVKAARLV VPEEVRWSGP LQFDHEEKEQ QAGHTYHIKP
VPEPEDYKNG VEQGLARIAD GTLSKIVLSR SLHLTSPEPI QTDELLRHLA QHNSHGYTFA
ADVSSQEETS PRRTLLGASP ELLVSRMGTQ VVSNPLAGSR PRSNDPVEDQ RRAAELLSSA
KDLHEHAVVA DAVAAALRPF CRTLEVPEKP SLIKTETMWH LSSVIKGELS DPSVTALELA
AALHPTPAVC GTPTDLAREA ILSIEPFDRG FFTGMVGWCD DAGDGEWIVT IRCAEAEERS
LRLYAGAGVV AGSKPEDELQ ETSAKFRTML RAMGVDHI