ID B8HVE1_CYAP4 Unreviewed; 309 AA.
AC B8HVE1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE Short=OSBS {ECO:0000256|HAMAP-Rule:MF_00470};
DE EC=4.2.1.113 {ECO:0000256|HAMAP-Rule:MF_00470};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
GN Name=menC {ECO:0000256|HAMAP-Rule:MF_00470};
GN OrderedLocusNames=Cyan7425_2232 {ECO:0000313|EMBL:ACL44593.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44593.1};
RN [1] {ECO:0000313|EMBL:ACL44593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44593.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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_00470}.
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_00470};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00470};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00470}.
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_00470}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 1 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00470}.
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DR EMBL; CP001344; ACL44593.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HVE1; -.
DR STRING; 395961.Cyan7425_2232; -.
DR KEGG; cyn:Cyan7425_2232; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_0_2_3; -.
DR OrthoDB; 9802699at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00165.
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:InterPro.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03320; OSBS; 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_00470; MenC_1; 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; IPR048639; MenC_N.
DR InterPro; IPR010196; OSB_synthase_MenC1.
DR NCBIfam; TIGR01927; menC_gam_Gplu; 1.
DR PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR Pfam; PF21508; MenC_N; 1.
DR Pfam; PF13378; MR_MLE_C; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00470};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00470}.
FT DOMAIN 116..215
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ SEQUENCE 309 AA; 34476 MW; 19BCD0B219E8B5F4 CRC64;
MYTVHFQRCD RPFRPPLHTH HGVWSVRQSI LVQLRDGDGR SGWGEIAPLS WFGSETLEQA
WEFCVQLPTQ IRRETIFSIP GSLPACQFGF ESAWEALNQD RINISIPALP HCGLLPAGTA
ALAQWPDLLS LGYRTLKWKM GVLPIAEELS IFRQLCQELP TGIQLRLDAN GGLSIASAHL
WLQTCDPTRV EFLEQPLPPP ELETMQELAR QYSTPLALDE SIANLQQLKA CYQQGWQGIY
VIKPAIAGSP AQLRQFLRSH SIDVVFSTVF EGAIGREAAL KIAAEFAQNG RAVGFGIHHW
FADSEPEGL
//
