(data stored in ACNUC1104 zone)

SWISSPROT: A4F763_SACEN

ID   A4F763_SACEN            Unreviewed;       331 AA.
AC   A4F763;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|HAMAP-Rule:MF_00470, ECO:0000256|SAAS:SAAS00050627};
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   ECO:0000313|EMBL:CAL99887.1};
GN   OrderedLocusNames=SACE_0541 {ECO:0000313|EMBL:CAL99887.1};
GN   ORFNames=A8924_0941 {ECO:0000313|EMBL:PFG93690.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99887.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99887.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99887.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93690.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93690.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
CC       {ECO:0000256|HAMAP-Rule:MF_00470, ECO:0000256|SAAS:SAAS00169585}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-
CC         carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689;
CC         EC=4.2.1.113; Evidence={ECO:0000256|HAMAP-Rule:MF_00470,
CC         ECO:0000256|SAAS:SAAS01117204};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={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
CC       4/7. {ECO:0000256|HAMAP-Rule:MF_00470,
CC       ECO:0000256|SAAS:SAAS00160640}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
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, ECO:0000256|SAAS:SAAS00555431}.
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DR   EMBL; AM420293; CAL99887.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93690.1; -; Genomic_DNA.
DR   STRING; 405948.SACE_0541; -.
DR   EnsemblBacteria; CAL99887; CAL99887; SACE_0541.
DR   KEGG; sen:SACE_0541; -.
DR   eggNOG; ENOG4107TCW; Bacteria.
DR   eggNOG; COG4948; LUCA.
DR   HOGENOM; HOG000249513; -.
DR   KO; K02549; -.
DR   OMA; AGWGEFS; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 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; IPR010196; OSB_synthase_MenC1.
DR   InterPro; IPR041338; OSBS_N.
DR   Pfam; PF18374; Enolase_like_N; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F763.
DR   SWISS-2DPAGE; A4F763.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00470, ECO:0000256|SAAS:SAAS00448201,
KW   ECO:0000313|EMBL:CAL99887.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00470,
KW   ECO:0000256|SAAS:SAAS00448198};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00470};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00470,
KW   ECO:0000256|SAAS:SAAS01101683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN       88    188       MR_MLE. {ECO:0000259|SMART:SM00922}.
FT   ACT_SITE    110    110       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   ACT_SITE    216    216       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       141    141       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       169    169       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       192    192       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
SQ   SEQUENCE   331 AA;  34560 MW;  85230BAA2A88BE75 CRC64;
     MDATGARIEL TDLDAVRVYG LPMRNRFRGI TVRQGVLLRG PAGWGEFCPF DDYGDAESVP
     WLATALEACA GDWPEPVRDS VPVNCTVPVV TPEKAHEIAA GSGCATAKVK VAESGRPPGE
     DVERVAAVRD ALGPGGAVRV DANAAWDVDT AVARIRELDR AAGGLEYVEQ PCPSVDELAA
     VRRRVEVRIA ADESIRRAED PMRVAVAGAA DVAVIKVSPL GGVRRALRVA EASGLPCVVS
     SAVESSVGLA AQLALAGALP ELPFACGLGT ITLLEGDVVA DSLVPSGGRL PVPRRPPEPT
     PALVAAATPP ADVQRRWLDR LRRVHALLPA G
//

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