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Database: UniProt
Entry: F7NKQ9_9FIRM
LinkDB: F7NKQ9_9FIRM
Original site: F7NKQ9_9FIRM 
ID   F7NKQ9_9FIRM            Unreviewed;       370 AA.
AC   F7NKQ9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491};
DE            EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491};
GN   ORFNames=ALO_13389 {ECO:0000313|EMBL:EGO63363.1};
OS   Acetonema longum DSM 6540.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Acetonema.
OX   NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63363.1, ECO:0000313|Proteomes:UP000003240};
RN   [1] {ECO:0000313|EMBL:EGO63363.1, ECO:0000313|Proteomes:UP000003240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63363.1,
RC   ECO:0000313|Proteomes:UP000003240};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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:EGO63363.1}.
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DR   EMBL; AFGF01000119; EGO63363.1; -; Genomic_DNA.
DR   RefSeq; WP_004096555.1; NZ_AFGF01000119.1.
DR   AlphaFoldDB; F7NKQ9; -.
DR   STRING; 1009370.ALO_13389; -.
DR   eggNOG; COG4948; Bacteria.
DR   OrthoDB; 9774531at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000003240; Unassembled WGS sequence.
DR   GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT   DOMAIN          143..235
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   370 AA;  41686 MW;  7D3F9E7B7A32BCE4 CRC64;
     MKITKVVLRK MKMDLKVPFV VSFGALKDKH FMAVEVHTKD HVGYGDCSAF SHPYYNEETI
     STAWHIIQDF LVPLLFSKEE ISRPEEVSEL FSHIRRNKMA KAALDCAIWD LYAKENNISV
     ARALGGTRDK IETGISIGIQ ESPDDLVRVV ENFMGEGYRR VKVKIEPGRD IKYLEAVRKR
     FGNIMLMADA NSAYTLKDID LFKELDHLDL IMIEQPLSHD DIVDHAKLQG ALKTRICLDE
     SIHSVDDARH AIELGSARTI NIKVARVGGL TEARKIHDLC ASHDIPVWCG GMLDTGIARA
     HNVAIASLPN YRFPGDVPAS DRYWHQDVIS PAMTIDRNAM IQVPDKPGIG FEPVPGLMEA
     FSYERKEILH
//
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