ID A0A096AIV4_9FIRM Unreviewed; 273 AA.
AC A0A096AIV4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Putative 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01660};
DE Short=SHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01660};
DE EC=4.2.99.20 {ECO:0000256|HAMAP-Rule:MF_01660};
GN Name=menH {ECO:0000256|HAMAP-Rule:MF_01660};
GN ORFNames=HMPREF0872_08075 {ECO:0000313|EMBL:KGF46516.1};
OS Veillonella montpellierensis DNF00314.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1401067 {ECO:0000313|EMBL:KGF46516.1, ECO:0000313|Proteomes:UP000029628};
RN [1] {ECO:0000313|EMBL:KGF46516.1, ECO:0000313|Proteomes:UP000029628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00314 {ECO:0000313|EMBL:KGF46516.1,
RC ECO:0000313|Proteomes:UP000029628};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5-
CC elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-
CC cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-
CC hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). {ECO:0000256|HAMAP-
CC Rule:MF_01660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-
CC carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-
CC carboxylate + pyruvate; Xref=Rhea:RHEA:25597, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:58689, ChEBI:CHEBI:58818; EC=4.2.99.20;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01660};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF46516.1}.
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DR EMBL; JRNT01000037; KGF46516.1; -; Genomic_DNA.
DR RefSeq; WP_038153143.1; NZ_JRNT01000037.1.
DR AlphaFoldDB; A0A096AIV4; -.
DR eggNOG; COG0596; Bacteria.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000029628; Unassembled WGS sequence.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR HAMAP; MF_01660; MenH; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022485; SHCHC_synthase_MenH.
DR NCBIfam; TIGR03695; menH_SHCHC; 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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01660};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_01660}; Reference proteome {ECO:0000313|Proteomes:UP000029628}.
FT DOMAIN 19..170
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 273 AA; 30762 MW; D8B3FEF567B86789 CRC64;
MRIVVDDISY YIHVIGQGKP LVCFHGFSES GNTWDGIEIP GYAMYRLDFI GHGQSDKPLD
TQIYQLPQLL RQLHIVIQAA VGASYSLMGY SMGARIALLY ALQYQHDIEA LILESGSVGI
QDPSARKLRF LQDEALAKKI VRNGRAWFRD TWSALPIFKT QQTLPLSVQD SIRRRRFHNE
PYALHHTLMG SGQGCMPYVG HRLDEIMCPS LYISGALDEK YSSLGEEVFK KAHSFSTALI
QNVGHNTHLE RPREFERIVA QFLHATTGPS NGS
//
