ID B9M1T0_GEODF Unreviewed; 597 AA.
AC B9M1T0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=2-oxoacid decarboxylase/dehydrogenase, putative {ECO:0000313|EMBL:ACM19226.1};
GN OrderedLocusNames=Geob_0864 {ECO:0000313|EMBL:ACM19226.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19226.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM19226.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001390; ACM19226.1; -; Genomic_DNA.
DR RefSeq; WP_012645955.1; NC_011979.1.
DR AlphaFoldDB; B9M1T0; -.
DR STRING; 316067.Geob_0864; -.
DR KEGG; geo:Geob_0864; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_7; -.
DR OMA; ANWYARH; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 65532 MW; A0EDDE17DD367AAD CRC64;
MAITTSDYLV QRLMDWGVRR VYGYPGDGIN GVMGALNRAQ EKIRFYQARH EEEAAFMACG
HAKFTGEVGI CIATSGPGAI HLLNGLYDAK MDHQPVVAIV GQQATTSLGA DYQQEVDLIS
LFKDVAHHFV QMATNPAQIR HLVDRAVRIA LAERTVTCII LPNDVQELEA VESPPRKHGA
TFTGIGFSRP EVVPKKDDLR KAADVLNAGR KIAILVGAGA LHATEEVVET AEKVGAGVAK
ALLGKAALPD DLPYVTGSIG LLGTKPSYEL MMNCDTFLMI GSGFPYSEFL PREGQARGVQ
IDIDPRMLSL RYPMEVNLQG DTALTLRALL PLLEKKTDRS WQDGVEANVR EWWQVMEARA
NVSATPINPQ RLFWELSSRL PDHAIITCDS GSAANWYARD LKIRRGMMAS LSGTLSTMCP
GIPYALAAKI NNPERVVISL VGDGAVQMLG LNGLITIAKY WREWCDPRLV IMVLNNEDLN
QVTWEQRVMN GDPKFMGSQD IPAFPYARYA QMLGLEGIEL RHPNEIGAAW DAALKAGKPV
VIDAHCDPEV PPLPPHITFE QAKGYMFSIF KGDPNLGGMV KQSAKQMMAN MLSRSEK
//