MENC_BACSU
ID MENC_BACSU Reviewed; 371 AA.
AC O34514;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:10194342};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000305};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:10194342};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:10194342};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000305};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000305};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933}; Synonyms=ytfD;
GN OrderedLocusNames=BSU30780;
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;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10194342; DOI=10.1021/bi990140p;
RA Palmer D.R., Garrett J.B., Sharma V., Meganathan R., Babbitt P.C.,
RA Gerlt J.A.;
RT "Unexpected divergence of enzyme function and sequence: 'N-acylamino acid
RT racemase' is o-succinylbenzoate synthase.";
RL Biochemistry 38:4252-4258(1999).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342). Does
CC not show detectable N-acylamino acid racemase (NAAAR) activity with N-
CC acetyl-S-methionine as substrate (PubMed:10194342).
CC {ECO:0000269|PubMed:10194342}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate
CC = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933,
CC ECO:0000269|PubMed:10194342};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P29208,
CC ECO:0000255|HAMAP-Rule:MF_01933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 150 sec(-1) with SHCHC as substrate.
CC {ECO:0000269|PubMed:10194342};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC {ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01933}.
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DR EMBL; AF008220; AAC00228.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15056.1; -; Genomic_DNA.
DR PIR; F69991; F69991.
DR RefSeq; NP_390956.1; NC_000964.3.
DR RefSeq; WP_004398737.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34514; -.
DR SMR; O34514; -.
DR STRING; 224308.BSU30780; -.
DR PaxDb; O34514; -.
DR PRIDE; O34514; -.
DR EnsemblBacteria; CAB15056; CAB15056; BSU_30780.
DR GeneID; 937201; -.
DR KEGG; bsu:BSU30780; -.
DR PATRIC; fig|224308.179.peg.3336; -.
DR eggNOG; COG4948; Bacteria.
DR InParanoid; O34514; -.
DR OMA; DIVDHRH; -.
DR PhylomeDB; O34514; -.
DR BioCyc; BSUB:BSU30780-MON; -.
DR BioCyc; MetaCyc:MON-13796; -.
DR SABIO-RK; O34514; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IGC:UniProtKB.
DR CDD; cd03317; NAAAR; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_01933; MenC_2; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR010197; OSB_synthase_MenC_2.
DR PANTHER; PTHR48073:SF5; PTHR48073:SF5; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01928; menC_lowGC/arch; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..371
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000171282"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-
FT Rule:MF_01933"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-
FT Rule:MF_01933"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-
FT Rule:MF_01933"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-
FT Rule:MF_01933"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208, ECO:0000255|HAMAP-
FT Rule:MF_01933"
SQ SEQUENCE 371 AA; 41629 MW; DC6996175BDB5833 CRC64;
MIEIEKITLY HLSMNLKKPF KNSIETLQER KFLIVEAIDT SGVTGWGEVS AFSSPWYTEE
TIGTCLHMLK DFFIPNVVGR EFNHPSEVPD SLARYKGNRM AKAGLESAVW DIYAKKKGVS
LAEALGGTRD KVPAGVVVGL APLDDMLKEI ESYQKEGYQR IKIKIQPGQD VELVKAIRSR
FPTIPLMADA NSSYELKDIS RLKELDDYHL MMIEQPLQAD DIVDHRHLQK HLKTAICLDE
SICSVDDARR AIELGSCKII NIKPSRVGGL TEALKIHDLC KEHHMQVWCG GMLETGISRA
QNVALASLPQ FTIPGDISSS SRYWDEDIVT PDIRIDNGFI SVSKQPGLGV EVNQDIMRKY
VTKMDVFTQH G
