ID A0A1B1APW1_9ACTN Unreviewed; 390 AA.
AC A0A1B1APW1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:ANP48596.1};
GN ORFNames=AVL59_02545 {ECO:0000313|EMBL:ANP48596.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP48596.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP48596.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP48596.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP016279; ANP48596.1; -; Genomic_DNA.
DR RefSeq; WP_067299576.1; NZ_JAGGLP010000022.1.
DR AlphaFoldDB; A0A1B1APW1; -.
DR STRING; 68214.AVL59_02545; -.
DR KEGG; sgs:AVL59_02545; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000092659; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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 Pyruvate {ECO:0000313|EMBL:ANP48596.1}.
FT DOMAIN 8..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 224..343
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 390 AA; 40468 MW; 4782493690042CC3 CRC64;
MTAEAAGGSE AFLAGLEAIG VSLVSGVPCS YFKEPIRRLE QHPRIRYVPA VNEGSALAIA
AGARLTGETA AVVAQNSGFG NLVNPLTSLA LPYRIPLLVF VSMRGWPTAD AGEPQHHWMG
KVVPPWLESL EVPYWWLTTD GPSPDAVVKE AGTVLESGRT AFVLVGKGAL KDAGAAPAPD
PAAPRASVPD RDDLVDAVLA EVREERILST TGYLSRTLYN RGDRPGNFYM QGSMGHVAGL
ALGAALARPE ERFVVLDGDG SALMHLGSLA TVGHFTPANL VHVVFDNQAY DSTGGQPTTS
ATTDFAAVAR ACGYRQVRRV GTAAGLRPAL RALLDAPGPG LLAVDGKVGG APCERASNSL
SVAGIATRFA AQHRSAGAHG GASGGHREQT
//
