ID R7A009_9FIRM Unreviewed; 373 AA.
AC R7A009;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:CDD36072.1};
GN ORFNames=BN600_00230 {ECO:0000313|EMBL:CDD36072.1};
OS Roseburia sp. CAG:309.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262945 {ECO:0000313|EMBL:CDD36072.1, ECO:0000313|Proteomes:UP000018292};
RN [1] {ECO:0000313|EMBL:CDD36072.1, ECO:0000313|Proteomes:UP000018292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:309 {ECO:0000313|Proteomes:UP000018292};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDD36072.1}.
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DR EMBL; CBGX010000334; CDD36072.1; -; Genomic_DNA.
DR AlphaFoldDB; R7A009; -.
DR STRING; 1262945.BN600_00230; -.
DR Proteomes; UP000018292; Unassembled WGS sequence.
DR GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR CDD; cd03371; TPP_PpyrDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR017684; Phosphono-pyrv_decarboxylase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03297; Ppyr-DeCO2ase; 1.
DR PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:CDD36072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018292}.
FT DOMAIN 10..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 212..341
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 373 AA; 41066 MW; 46D74DC27AD646AD CRC64;
MQVETFVNML NVDFYTGVPD SLLKPLCNYL MDTYGIDSRH HMIAANEGNC AALAAGYHLA
TGKVPAVYMQ NSGEGNIINP LASLLNDKVY GIPMIFIVGW RGEPGVHDEP QHIYQGEVTV
KLLEDMDVAA YVVTKETTEE ELDAQMQVFR SLLAKGKDVA FVVKKGALSF GKNVEYSNKN
HMRREEIIEH IVNVSKEDPI LSTTGKASRE LFEIREKNGQ SHKYDFLTVG SMGHTSSIAL
GVALQKTDKR IWCIDGDGAM LMHMGAMAVI GANRPSNLVH IVINNGAHET VGGLPTVAAE
LDLVKMAEAC GYPYAVCVKD FEQLDKELQA AKQRNALTLI EAECAIGARE DLGRPTTAAL
ENKENFMRYL QEE
//
