ID D3AC94_9CLOT Unreviewed; 390 AA.
AC D3AC94;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:EFD00572.1};
DE EC=4.1.1.82 {ECO:0000313|EMBL:EFD00572.1};
GN Name=aepY {ECO:0000313|EMBL:EFD00572.1};
GN ORFNames=CLOSTHATH_01222 {ECO:0000313|EMBL:EFD00572.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFD00572.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFD00572.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFD00572.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) 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:EFD00572.1}.
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DR EMBL; ACIO01000079; EFD00572.1; -; Genomic_DNA.
DR AlphaFoldDB; D3AC94; -.
DR HOGENOM; CLU_042853_0_0_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:UniProtKB-EC.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:EFD00572.1};
KW Pyruvate {ECO:0000313|EMBL:EFD00572.1}.
FT DOMAIN 27..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..359
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 390 AA; 43025 MW; 600E72F18B05BBF6 CRC64;
MLLNYCIGKF LERKNKIMKA NKLAEILGAD FYTGVPDSQL KALCNYLMDT YGIDPKHHII
AANEGNCTAL AAGYHLATGK IPVVYMQNSG EGNIINPVAS LLNDKVYAIP VIFIVGWRGE
PGTYDEPQHI YQGEVTIKLL EDMGIKPFII FKDTTNEEVK STMEYFGEIL KSGKSVAFVV
CKDSISYDGK TKYSNNNKMS REEVIRHITK ITGEDPVIST TGKASRELFE IRKQDDQSHK
YDFLTVGSMG HSSSIALGIA VNKPDTKIWC IDGDGAVLMH MGSMAVLGNY KPANMVHIII
NNGAHETVGG MPTVAGSIDL VGIAKSCGYP YAVCVDNFEK LDDELNMAKE RNVMSMIEVK
CSIASRDNLG RPTTTAFENK QNFMNYLNLL
//
