ID   C0ZRF4_RHOE4            Unreviewed;       371 AA.
AC   C0ZRF4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|NCBIfam:TIGR01928};
DE            EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|NCBIfam:TIGR01928};
GN   OrderedLocusNames=RER_09960 {ECO:0000313|EMBL:BAH31704.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31704.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|EMBL:BAH31704.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT   strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR   EMBL; AP008957; BAH31704.1; -; Genomic_DNA.
DR   RefSeq; WP_020906340.1; NC_012490.1.
DR   AlphaFoldDB; C0ZRF4; -.
DR   KEGG; rer:RER_09960; -.
DR   PATRIC; fig|234621.6.peg.1453; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_4_11; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000002204; Chromosome.
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   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N.
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; SFLDS00001; Enolase; 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   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002204}.
FT   DOMAIN          142..235
FT                   /note="Mandelate racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   371 AA;  39931 MW;  DB9CDD75F5B629C3 CRC64;
     MKIDGVELRR AAMPLKAPFR TSFGTETTKD VLFVKVVTSE SAGWGECVAM SEPRYCSEYT
     DGAAEVLRKF LIPSLGELTD PDVHALSATM EQFAGHPMAK AALETAFLDA ELRAAGTSMS
     SYLGAVVDRV PAGVSVGIKN SIDELLEEVG GFLDAGYLRI KLKIEPGWDI EPVRAVRERF
     GDDVLLQVDA NTAYTLADAR HLQRLDDFDL LLIEQPLPEE ELRGHARLAE MMRTPVCLDE
     SITSAKVTAD ALAIGACSVV NIKSGRVGGY LESRRIHDVC KANGIAVWCG GMLETGIGRA
     ANVALAALPG FVLPGDTSAS DRYFAEDITE PFVLDSGYVK VPEGPGIGVE PIPDLLEAIT
     TSVEWIGMDR L
//