(data stored in SCRATCH zone)

SWISSPROT: A0KFN5_AERHH

ID   A0KFN5_AERHH            Unreviewed;       309 AA.
AC   A0KFN5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
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:ABK37251.1};
GN   OrderedLocusNames=AHA_0528 {ECO:0000313|EMBL:ABK37251.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37251.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37251.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37251.1; -; Genomic_DNA.
DR   RefSeq; WP_011704501.1; NC_008570.1.
DR   RefSeq; YP_855061.1; NC_008570.1.
DR   STRING; 380703.AHA_0528; -.
DR   EnsemblBacteria; ABK37251; ABK37251; AHA_0528.
DR   GeneID; 4488868; -.
DR   KEGG; aha:AHA_0528; -.
DR   PATRIC; fig|380703.7.peg.521; -.
DR   eggNOG; ENOG4105DNI; Bacteria.
DR   eggNOG; COG1441; LUCA.
DR   HOGENOM; HOG000271247; -.
DR   KO; K02549; -.
DR   OMA; YEANRDG; -.
DR   BioCyc; AHYD380703:G1G7B-529-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000000756; 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:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR010196; OSB_synthase_MenC1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFN5.
DR   SWISS-2DPAGE; A0KFN5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00470, ECO:0000256|SAAS:SAAS00448201,
KW   ECO:0000313|EMBL:ABK37251.1};
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:UP000000756}.
FT   DOMAIN      107    201       MR_MLE. {ECO:0000259|SMART:SM00922}.
FT   ACT_SITE    128    128       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   ACT_SITE    226    226       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       156    156       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       182    182       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
FT   METAL       205    205       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00470}.
SQ   SEQUENCE   309 AA;  34454 MW;  A5712F9BA78A23F2 CRC64;
     MTLALYRYQL PFTQPLTFHG KVEVAREGLL VRVDDGWGEI APLPGFSRES LAEAQAEAIA
     SLEQLAAGQE IAPQLPSVQF GLDCARRCWP AQTTPLPEPY PLIQGSPQEL LKHWKNWLHT
     TPSKAKLKVA RYPMRDELAL IRLLCDRIPT LKLVLDANQG WTREEAWAFC GHLDPNRIEY
     LEDPCANFAD IAFVANRTGM PVAIDELLAQ GKPWEPIPQL RALVLKPTLL GSLAHCEALV
     ARARELRLKV IVSSCFESGL GLNQLFHLAG EWAPDQAPGL DTRRWLAADL LDATGKPDLS
     LLEPLFHRD
//

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