ID L1MCC2_9BACT Unreviewed; 509 AA.
AC L1MCC2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Putative 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase {ECO:0000313|EMBL:EKX88644.1};
GN ORFNames=HMPREF9999_01685 {ECO:0000313|EMBL:EKX88644.1};
OS Alloprevotella sp. oral taxon 473 str. F0040.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX88644.1, ECO:0000313|Proteomes:UP000010460};
RN [1] {ECO:0000313|EMBL:EKX88644.1, ECO:0000313|Proteomes:UP000010460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0040 {ECO:0000313|EMBL:EKX88644.1,
RC ECO:0000313|Proteomes:UP000010460};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:EKX88644.1}.
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DR EMBL; AMEK01000080; EKX88644.1; -; Genomic_DNA.
DR RefSeq; WP_009437641.1; NZ_KB290717.1.
DR AlphaFoldDB; L1MCC2; -.
DR STRING; 1035197.HMPREF9999_01685; -.
DR PATRIC; fig|1035197.3.peg.1400; -.
DR eggNOG; COG1165; Bacteria.
DR HOGENOM; CLU_006051_3_0_10; -.
DR OrthoDB; 9791859at2; -.
DR Proteomes; UP000010460; Unassembled WGS sequence.
DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR004433; MenaQ_synth_MenD.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
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; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF004983; MenD; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000010460}.
FT DOMAIN 10..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
SQ SEQUENCE 509 AA; 56730 MW; 3BC65E4474C3546F CRC64;
MYSKKANINL LTARLIAHDI RDIVVCPGSR NAPIVHNLYE AGSKFQLHPI TDERSAAFVA
IGLWIKRKRP IAICVTSGSA LLNCLPGIAE AAFRHIPLVM ISADRPLSLQ GQLDGQTIPQ
QGACLPYARC WQIDEIEEDA QAWEVNHDLQ TAFAALSDNG GQPIHLNIPI SEPLFEFTTK
ELPKVEVSTK VNKPVAKLPK HWQELLYNAH LPLLIVGQYE ESFIPAIQQL RANNQLLVYA
ENISNQQDAR MALWLDEQKL SPDSVIHIGG CLVNKFFKQH LRTISQLPVL RIDETDECPD
TFFQKAEKLT CNPAEILQQL VDTLPTKNEV AAAYSQLRPP EHTFDYPIEA MFVGNSTAVR
WTNRQWPVLN VPIYCNRGTN GIEGSLSTAA GYSLVAEEKI LCIIGDLSFF YDANGLWNQH
LDGKLRILLI NNQCGAIFHH LPGLKETPAL PHLVAAAHHN SAKGIAESYH CTYLSAESSC
VEEDAHHLLI KLLNIESTRP VILEVFTPI
//