ID F8IE86_ALIAT Unreviewed; 278 AA.
AC F8IE86;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ECO:0000313|EMBL:AEJ43928.1};
GN OrderedLocusNames=TC41_2016 {ECO:0000313|EMBL:AEJ43928.1};
OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ43928.1, ECO:0000313|Proteomes:UP000000292};
RN [1] {ECO:0000313|EMBL:AEJ43928.1, ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ43928.1,
RC ECO:0000313|Proteomes:UP000000292};
RX PubMed=21914900; DOI=10.1128/JB.05709-11;
RA Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT 4-1.";
RL J. Bacteriol. 193:5602-5603(2011).
RN [2] {ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA Chen Y., He Y., Dong Z., Hu S.;
RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT 1.";
RL Submitted (JUN-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002902; AEJ43928.1; -; Genomic_DNA.
DR RefSeq; WP_014464776.1; NC_017167.1.
DR AlphaFoldDB; F8IE86; -.
DR STRING; 1048834.TC41_2016; -.
DR ESTHER; aliat-f8ie86; MenH_SHCHC.
DR KEGG; aad:TC41_2016; -.
DR PATRIC; fig|1048834.4.peg.1905; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_50_4_9; -.
DR OrthoDB; 9808398at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000000292; Chromosome.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR000639; Epox_hydrolase-like.
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 PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AEJ43928.1};
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}.
FT DOMAIN 24..260
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 278 AA; 30582 MW; 5E99AA5EBF09F48B CRC64;
MKRVALVRGV RYAYRLVPGG EPCLFLHGFT GAGDVFLPVL ERLAGLGCRP CAILPDLLGH
GASDVPDDAG RYSMDETVRD LDALLEELRI PSCQVVGYSM GGRVALAFAI AHPERVRALV
LESASPGIED ASEREARRRE DDALADEIEA RGLEWFVSEW ERRPIFATHE ALPEEEKARQ
RAIRLSGSAR GYAQSLRGLG TGRQPSYWGA LGRLRMPVAL VTGALDAKFT GMAKRMQSRL
QNAVHVAIES AGHTPHLEQP DRFATWLAQF FSSQGRLH
//
