ID   A0A0G1BEX5_9BACT        Unreviewed;       742 AA.
AC   A0A0G1BEX5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:KKS44916.1};
DE   Flags: Fragment;
GN   ORFNames=UV07_C0001G0036 {ECO:0000313|EMBL:KKS44916.1};
OS   Candidatus Azambacteria bacterium GW2011_GWB1_42_17.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618615 {ECO:0000313|EMBL:KKS44916.1, ECO:0000313|Proteomes:UP000033986};
RN   [1] {ECO:0000313|EMBL:KKS44916.1, ECO:0000313|Proteomes:UP000033986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKS44916.1}.
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; LCDB01000001; KKS44916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1BEX5; -.
DR   PATRIC; fig|1618615.3.peg.36; -.
DR   Proteomes; UP000033986; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR   CDD; cd08182; HEPD; 1.
DR   CDD; cd03371; TPP_PpyrDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR017684; Phosphono-pyrv_decarboxylase.
DR   InterPro; IPR035873; PhpC.
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; PF00465; Fe-ADH; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:KKS44916.1}.
FT   DOMAIN          18..126
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          244..358
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          395..739
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   NON_TER         742
FT                   /evidence="ECO:0000313|EMBL:KKS44916.1"
SQ   SEQUENCE   742 AA;  81010 MW;  804039F208193710 CRC64;
     MHTHRGTFGF EFMISPKIFY DLLIKNGVGF FSGVPDSLLK DFSAYIADNA KPNYHVIAAN
     EGGAVALAAG YHLATGKIGL VYMQNSGEGN AVNPLVSLAD PEVYGIPMLL LIGWRGEPGV
     HDEPQHIKQG KITLKILKTL GIPFEILPDS ATAVKKAIKR AIDHIKTSCA PFTFVVRRGT
     FELYINRKTV QKVKNQLSRE KAIEIITDEL NDGEILISTT GKTSRELFEV RESADYGHEK
     DFLTVGSMGH SSQIALGVAL AKPERQVYCL DGDGALIMHM GALAIIGNMA PKNFKHIVLN
     NHAHESVGGQ STAAFSMNIP AIAQFCSYKR IFRASGADEL KQVLKNFKKA SGPALLEITI
     KQGSRSDLGR PALSPKENKN LFMDFINHGS QTLLAAEKLK NFFEDKKVRR IFLVTGGKSY
     ITSGAEQMFR KILLSYEVTK FSGFNPNPKL DDVERGINIF KKKKYDAVVA IGGGSAIDMA
     KLINIFSAQH GAPIDYVTLK KVIKNTGKPL AAVPTTAGSG SEATHFAVVY VGGKKYSVAH
     ESMLPAEAIV EPILTMNMPP YLAAVSGIDA LSQAIESYWC VSATNTSKRF AERAIRLILD
     NLVRSVKKPT LESRSAMARA SHLAGKAINI TKTTAPHAIS YFFTSRFNIP HGHAVALTLG
     KMFIYNNRAN RAMTDLLRLL GVSNAGAASR KIAGIMKQIG LETKLHKLGV SRSDIDLAVK
     SVNVERLKNN PKKMTERDIR KI
//