ID A0A150KKE4_9BACI Unreviewed; 370 AA.
AC A0A150KKE4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|HAMAP-Rule:MF_01933};
DE Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_01933};
DE Short=OSBS {ECO:0000256|HAMAP-Rule:MF_01933};
DE EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|HAMAP-Rule:MF_01933};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_01933};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000256|HAMAP-Rule:MF_01933};
GN ORFNames=B4102_4166 {ECO:0000313|EMBL:KYC84862.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYC84862.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYC84862.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYC84862.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000256|HAMAP-
CC Rule:MF_01933}.
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:0000256|HAMAP-Rule:MF_01933};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968,
CC ECO:0000256|HAMAP-Rule:MF_01933};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC {ECO:0000256|HAMAP-Rule:MF_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01933}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01933}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC84862.1}.
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DR EMBL; LQYN01000168; KYC84862.1; -; Genomic_DNA.
DR RefSeq; WP_066235857.1; NZ_LQYN01000168.1.
DR AlphaFoldDB; A0A150KKE4; -.
DR STRING; 46224.B4102_4166; -.
DR PATRIC; fig|46224.3.peg.1966; -.
DR OrthoDB; 9774531at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000075666; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR CDD; cd03317; NAAAR; 1.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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; IPR047585; MenC.
DR InterPro; IPR010197; OSBS/NAAAR.
DR NCBIfam; TIGR01928; menC_lowGC_arch; 1.
DR PANTHER; PTHR48073:SF5; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDG00180; muconate_cycloisomerase; 1.
DR SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01933, ECO:0000313|EMBL:KYC84862.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01933};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01933};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01933}; Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT DOMAIN 142..234
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
SQ SEQUENCE 370 AA; 41871 MW; 19B34CA6EEEA0FF6 CRC64;
MRIHEVNIFI IKMPLKQPFT TALETVNERE GIILEVIDEQ GAKGYGEVVA FSTPWYTEET
VKTCYHMLTD LLIPLVLDKQ INHPNDLQMI FNHIRGNHMA KAGLETAIWD LYSKLESKPL
WTVMNGVRDE VPAGVVVGTA NINDAIEQIH VYLEDGYERV KVKIKPGKDY QLIKEIRTYF
PKLALMADAN SSYTLNDMDV LKSLDEFNLL MIEQPLAVDD IVEHSILQKE LKTPICLDES
IITYHDAESA IRLNSCGVIN IKIGRVGGLR NAIAIHDLCQ KNDIQVWCGG MIEFGVSRAH
NLALSTKEGF TIPGDLSASS RFWEEDIIYP QVEVANGKVK VPNQPGIGFD INFNRLYRVT
TYRENINCKH
//
