MENC_BDEBA
ID MENC_BDEBA Reviewed; 330 AA.
AC Q6MQC7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Bd0547 {ECO:0000312|EMBL:CAE78520.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
RN [2] {ECO:0007744|PDB:3CAW}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
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=53 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; BX842647; CAE78520.1; -; Genomic_DNA.
DR RefSeq; WP_011163122.1; NC_005363.1.
DR PDB; 3CAW; X-ray; 1.87 A; A/B=1-330.
DR PDBsum; 3CAW; -.
DR SMR; Q6MQC7; -.
DR STRING; 264462.Bd0547; -.
DR EnsemblBacteria; CAE78520; CAE78520; Bd0547.
DR KEGG; bba:Bd0547; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_878898_0_0_7; -.
DR OrthoDB; 1825904at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; Q6MQC7; -.
DR Proteomes; UP000008080; 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: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 SUPFAM; SSF51604; SSF51604; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..330
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455092"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P29208"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24872444,
FT ECO:0007744|PDB:3CAW"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24872444,
FT ECO:0007744|PDB:3CAW"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24872444,
FT ECO:0007744|PDB:3CAW"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:3CAW"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:3CAW"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:3CAW"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3CAW"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:3CAW"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3CAW"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3CAW"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:3CAW"
SQ SEQUENCE 330 AA; 37401 MW; E67D64135E164929 CRC64;
MIKISYSPYT LKPVQSLNAA TAATAREGVL LKVEWNDGLY GFADLHPWPE LGDLSLEEQL
SDLRMGRMTT QIEQSIWLAR RDALLRKEKK HVFDGGEKIK NNYLLSHFQD LKPGFLDGLK
NEGYNTVKVK MGRDLQKEAD MLTHIAASGM RMRLDFNALG SWQTFEKFMV NLPLTVRPLI
EYVEDPFPFD FHAWGEARKL AKIALDNQYD KVPWGKIASA PFDVIVIKPA KTDVDKAVAQ
CQKWNLKLAV TSYMDHPVGV VHAVGVAMEL KDKYGDMILE SGCLTHRLYQ MDSFAAELST
QGPYLLKNKG TGVGFDKLLE ALTWYQLKVR
