GenomeNet

Database: UniProt
Entry: L1MCC2_9BACT
LinkDB: L1MCC2_9BACT
Original site: L1MCC2_9BACT 
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}.
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; 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
//
DBGET integrated database retrieval system