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Database: UniProt
Entry: A9FVI2_SORC5
LinkDB: A9FVI2_SORC5
Original site: A9FVI2_SORC5 
ID   A9FVI2_SORC5            Unreviewed;       595 AA.
AC   A9FVI2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:CAN92279.1};
DE            EC=1.2.3.3 {ECO:0000313|EMBL:CAN92279.1};
GN   OrderedLocusNames=sce2120 {ECO:0000313|EMBL:CAN92279.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN92279.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN92279.1, ECO:0000313|Proteomes:UP000002139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AM746676; CAN92279.1; -; Genomic_DNA.
DR   RefSeq; WP_012234754.1; NC_010162.1.
DR   AlphaFoldDB; A9FVI2; -.
DR   STRING; 448385.sce2120; -.
DR   KEGG; scl:sce2120; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_7; -.
DR   OrthoDB; 2254214at2; -.
DR   BioCyc; SCEL448385:SCE_RS10900-MONOMER; -.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0047112; F:pyruvate oxidase activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:CAN92279.1};
KW   Pyruvate {ECO:0000313|EMBL:CAN92279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..328
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..542
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   595 AA;  65387 MW;  EADAB8A06245D9E4 CRC64;
     MAQTVGEFLL RRLVAWGVRR VYAYPGDGIN GIVGAFHRVP DLRFIQVRHE EMAAFMACAH
     AKFTGEVGVC LATSGPGAIH LLNGLYDAKL DHQPVVAIVG QQDRAALGGH YQQEVDLVTL
     FKDVAHEYVQ MASSPAQMRH LIDRAMRIAK AERTVTCVIV PKDVQELDAV EQPPHAHGTV
     HSGIGYSSPR VVPKEEDLRR AADVLNAGKR VAMLIGQGAL GAAPEIVRAA EILGCGVAKA
     LLGKAALPDD LPWVTGAIGL LGTKPSWEMM ANCDTLFMVG SNFPYPEFLP EEGKARGVQI
     DIDGRMLGLR YPMEVNLIGD CAETLRALIP YLKLKTDRSW RRKLEESVAD WWKVLEARAM
     NDADPLNPQR VYWELSPRLP DGCILTADSG TSANWYARDI KIRAGMMASL SGTLATMGPA
     MPYAVAAKFA FPDRPVVAMV GDGAMQMNGI NTLITVAKYW REWKDPRLVV LVLNNRDLNM
     VTWELRAMSG DPKLEASQTL PDFPYAAYAE ALGLRGVRID RPDQCARTWD EAFRVDRPVV
     VEAITDPEVP PLPPHITVKQ AAMLTSALLR GDPGGRGIVR QAYRDMIESW IPHRG
//
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