MENC_DESPS
ID MENC_DESPS Reviewed; 368 AA.
AC Q6ARP5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000303|PubMed:24872444};
DE Short=OSB synthase {ECO:0000250|UniProtKB:P29208};
DE Short=OSBS {ECO:0000303|PubMed:24872444};
DE EC=4.2.1.113 {ECO:0000269|PubMed:24872444};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000250|UniProtKB:P29208};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000250|UniProtKB:P29208};
GN Name=menC {ECO:0000250|UniProtKB:P29208};
GN OrderedLocusNames=DP0251 {ECO:0000312|EMBL:CAG34980.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
RN [2] {ECO:0007744|PDB:2PGE}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-368, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=24872444; DOI=10.1073/pnas.1318703111;
RA Odokonyero D., Sakai A., Patskovsky Y., Malashkevich V.N., Fedorov A.A.,
RA Bonanno J.B., Fedorov E.V., Toro R., Agarwal R., Wang C., Ozerova N.D.,
RA Yew W.S., Sauder J.M., Swaminathan S., Burley S.K., Almo S.C.,
RA Glasner M.E.;
RT "Loss of quaternary structure is associated with rapid sequence divergence
RT in the OSBS family.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8535-8540(2014).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Does
CC not show N-succinylamino acid racemase (NSAR) activity with N-succinyl-
CC L-phenylglycine as substrate (PubMed:24872444).
CC {ECO:0000269|PubMed:24872444}.
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:0000269|PubMed:24872444};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24872444};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 17 sec(-1) with SHCHC as substrate.
CC {ECO:0000269|PubMed:24872444};
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}.
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000250|UniProtKB:P29208}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24872444}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 1 subfamily. {ECO:0000305}.
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DR EMBL; CR522870; CAG34980.1; -; Genomic_DNA.
DR PDB; 2PGE; X-ray; 1.60 A; A=2-368.
DR PDBsum; 2PGE; -.
DR SMR; Q6ARP5; -.
DR STRING; 177439.DP0251; -.
DR DNASU; 2946281; -.
DR EnsemblBacteria; CAG34980; CAG34980; DP0251.
DR KEGG; dps:DP0251; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_0_0_7; -.
DR OMA; INGLVWM; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q6ARP5; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..368
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455093"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2PGE"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2PGE"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:2PGE"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2PGE"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2PGE"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2PGE"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:2PGE"
SQ SEQUENCE 368 AA; 40565 MW; 5D12A6708F06B389 CRC64;
MSGMELSYRR SDLIFKRPAG TSRGVLTSKP TWFVRLDIDG HGGQGEVSLI PGLSLDPEEQ
IGRELDLLAR RLRAEEPIRL RQFLAERGGA DFSDYRSVLT DIAGILDSWQ VSTDGRFPAL
RFALEMALLD LLSGGRQEWF ASDFTRGEKR IPVNGLIWMG EAAFMQEQIE AKLAEGYGCL
KLKIGAIDFD KECALLAGIR ESFSPQQLEI RVDANGAFSP ANAPQRLKRL SQFHLHSIEQ
PIRQHQWSEM AALCANSPLA IALDEELIGL GAEQRSAMLD AIRPQYIILK PSLLGGFHYA
GQWIELARER GIGFWITSAL ESNLGLAAIA QWTALYQPTM PQGLGTGQLY TNNLPSNLAV
DGGLLGVS
