ID A0A1Z4V2L1_9CYAN Unreviewed; 569 AA.
AC A0A1Z4V2L1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE Short=SEPHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE EC=2.2.1.9 {ECO:0000256|HAMAP-Rule:MF_01659};
GN Name=menD {ECO:0000256|HAMAP-Rule:MF_01659};
GN ORFNames=NIES806_19640 {ECO:0000313|EMBL:BAZ85760.1};
OS Dolichospermum compactum NIES-806.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Dolichospermum; Dolichospermum compactum.
OX NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ85760.1, ECO:0000313|Proteomes:UP000218702};
RN [1] {ECO:0000313|EMBL:BAZ85760.1, ECO:0000313|Proteomes:UP000218702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ85760.1,
RC ECO:0000313|Proteomes:UP000218702};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01659};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01659}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01659}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01659}.
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DR EMBL; AP018316; BAZ85760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4V2L1; -.
DR OrthoDB; 9791859at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER00164.
DR Proteomes; UP000218702; Chromosome.
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 CDD; cd07037; TPP_PYR_MenD; 1.
DR CDD; cd02009; TPP_SHCHC_synthase; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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_TPP-bd.
DR NCBIfam; TIGR00173; menD; 1.
DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01659};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01659};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01659}; Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01659}.
FT DOMAIN 15..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..400
FT /note="Menaquinone biosynthesis protein MenD middle"
FT /evidence="ECO:0000259|Pfam:PF16582"
FT DOMAIN 434..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 569 AA; 63980 MW; 77CF801CC980A0F4 CRC64;
MQLTFNNLNL LWSYVLTETL KRLGLNCAVI CPGSRSTPLT IAFVQQIPDI EAIPILDERS
AAFFALGQAK VTGKPVVLVC TSGTAGANFY PAVIEARESR VPLLILTTDR PAELRNCHSG
QTIDQVKLYG NYPNWQGELA TPSLDVGMLD YLRQTVIYAW ERCQFPNSGA VHLNIPFRDP
LAPIPDGTEF TLDVEDFFAG IVSTPLPITS YQLPITNYQK GIIIAGVAQP QAPEDYCRAI
AHLSQTLQWP VLAEGVSPVR NYADLNPYII STYDIILRNQ NLAQELTPEV VIQIGEMPTS
KELRNWLTNA NPQRFVIDNC DQNLDPLHGK TTHLRISVTE IGKLEIGNLA ENEYLQKWST
AEKQVRKNID DDLENVDELI ESKVAWLISQ ILPPQTPLFI ANSMPVRDVE FFWKPNNLRI
KPYFNRGANG IDGTLSTALG IAHHQQSSVM LTGDLSLLHD TNGFLISNKF IGHLTIILIN
NNGGGIFEML PIAKFNPPFE EFFATPQNID FSKLCATYNV QHKLINSWEE LANRLKYLPK
TGIRVLEVKT NRKRDVMWRK ENLTKFGNW
//
