(data stored in SCRATCH zone)

SWISSPROT: A1SE16_NOCSJ

ID   A1SE16_NOCSJ            Unreviewed;       320 AA.
AC   A1SE16;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-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   OrderedLocusNames=Noca_0509 {ECO:0000313|EMBL:ABL80051.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL80051.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL80051.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
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; CP000509; ABL80051.1; -; Genomic_DNA.
DR   STRING; 196162.Noca_0509; -.
DR   EnsemblBacteria; ABL80051; ABL80051; Noca_0509.
DR   KEGG; nca:Noca_0509; -.
DR   eggNOG; ENOG4108IDS; Bacteria.
DR   eggNOG; COG4948; LUCA.
DR   HOGENOM; HOG000249513; -.
DR   KO; K02549; -.
DR   OMA; AGWGEFS; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000000640; Chromosome.
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; A1SE16.
DR   SWISS-2DPAGE; A1SE16.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00470,
KW   ECO:0000256|SAAS:SAAS00448201};
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:UP000000640}.
FT   DOMAIN       80    180       MR_MLE. {ECO:0000259|SMART:SM00922}.
FT   ACT_SITE    102    102       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   ACT_SITE    208    208       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       133    133       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       161    161       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       184    184       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
SQ   SEQUENCE   320 AA;  33888 MW;  D737898A4EE324EE CRC64;
     MGMIVWSVPM RTRFRGITVR EGVLLRGPAD AERPGWGEWS PFLEYDAAVA EPWLRCAEEA
     AAGDWPAPLR DRVPVNVTVP AVGPQQAHAI VLAGGCRTAK VKVAEPGQTA ADDQARLEAV
     RDALGADGRV RIDVNGLWDL DTAVASIPVL DRAAGGLEYV EQPCASVEDL AAVRRRVDVP
     IAADESIRRA ADPYRVRDLE AADVAVLKVQ PLGGVRACLR IAEDIGLPVV VSSALETSVG
     IAAGVALAAA LPELPYACGL ATVQLLTADV VTESLLPVGG ELPVRAVQVD ESLAPADPDR
     VAHWEARLAE VRALRQDRPS
//

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