MEND_CROS5
ID MEND_CROS5 Reviewed; 585 AA.
AC B1WZR3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659};
GN Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; OrderedLocusNames=cce_1865;
OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS ATCC 51142)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX NCBI_TaxID=43989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51142 / BH68;
RX PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT important in the marine nitrogen cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation
CC of 2-oxoglutarate and the subsequent addition of the resulting succinic
CC semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-
CC succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-
CC hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2;
CC Xref=Rhea:RHEA:25593, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29780, ChEBI:CHEBI:58818; EC=2.2.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01659};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01659}.
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DR EMBL; CP000806; ACB51215.1; -; Genomic_DNA.
DR RefSeq; WP_009545677.1; NC_010546.1.
DR AlphaFoldDB; B1WZR3; -.
DR SMR; B1WZR3; -.
DR STRING; 43989.cce_1865; -.
DR EnsemblBacteria; ACB51215; ACB51215; cce_1865.
DR KEGG; cyt:cce_1865; -.
DR eggNOG; COG1165; Bacteria.
DR HOGENOM; CLU_006051_3_0_3; -.
DR OMA; FCNRGTS; -.
DR OrthoDB; 897995at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000001203; Chromosome circular.
DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:InterPro.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01659; MenD; 1.
DR InterPro; IPR004433; MenaQ_synth_MenD.
DR InterPro; IPR032264; MenD_middle.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR42916; PTHR42916; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF16582; TPP_enzyme_M_2; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF004983; MenD; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00173; menD; 1.
PE 3: Inferred from homology;
KW Magnesium; Manganese; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..585
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="PRO_1000187063"
SQ SEQUENCE 585 AA; 66702 MW; 4D6CF162943C351A CRC64;
MQLDFRNINT LWSSIIVETL SRLGLTTAVI CPGSRSTPLT VAFASHSKID TIPILDERSA
AFFALGIAKR THLPVALICT SGTAGANFYP AVIEGKESQV PLLIFTADRP PELRNCHAGQ
TIDQVKLYGN YCNWYIELSL PSVEIRLLSY LRQTIIAAWD HALVPYKGIV HLNCPFREPL
APIIEPNIAS LCTEVNFDNF FLNIYESNKK RLRTDYLYDH LNHWLSQANG IIIAGVGNSN
NTDLYCNQIF RLSTLLNYPV LAEALCPFRN HAQGFPNLIN TYDILLRNQK LADELVPDVV
IQIGEFPTSK QLREWLTHHQ VQHWVIDSRP DSLDPLHNNT YYIRTDIHDL EMEYNKQCIP
GKQDLSYLQQ WKKINKIINR NIKTTLDKTN ELIEAKLPFI LSKNLQDKTS IFIANSMPVR
YAEFFWMPNK GQFMPYFNRG ANGIEGTLST ALGVAYKAKS SLLITGDLAL LHDTNGWLIR
QHFQGHLTII LINNNGGGIF EMLPIAKEES VFESYFATPQ NINFSQLCST YNVEHILIKN
WTQLKRLLNP LPSTGIRVLE LQTDRKKDAL WLQDNMKKLS MIDNK
