ID D9Y0L4_9ACTN Unreviewed; 605 AA.
AC D9Y0L4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Pyruvate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:EFL42905.1};
GN ORFNames=SSRG_05709 {ECO:0000313|EMBL:EFL42905.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL42905.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL42905.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL42905.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-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; GG657758; EFL42905.1; -; Genomic_DNA.
DR RefSeq; WP_004935267.1; NZ_GG657758.1.
DR AlphaFoldDB; D9Y0L4; -.
DR STRING; 467200.SSRG_05709; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000002968; Unassembled WGS sequence.
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 Pyruvate {ECO:0000313|EMBL:EFL42905.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 605 AA; 65758 MW; 4C99DABC34868B3A CRC64;
MKVSDYVLQR LREWEVDHVF SYAGDGINGL LAAWGRAENR PKFVQARHEE MAAFEAVGYA
KFSGKVGVCA ATSGPGAIHL LNGLYDAKLD RVPVVAIVGQ TNRSAMGGSY QQEVDLLSLY
KDVASDFCEM VTVPEQLPNV IDRAVRTAYG RRTVTAVIIP ADVQELDYSP PAHAFKMVPS
SLGTARYAPV PADEDLARAA EVLNAGEKVA VLVGQGARGA RAEVEAVADL LGAGVAKALL
GKDVLPDDQP YVTGSIGLLG TRPSYELMMD CDTLLVIGSS FPYTQFLPEF DQARAVQIDI
DPHNIGMRYP FEVNLVGDAR RTLENLLPLL RRKKHGSWRK KIEKDTARWW DVMERRAAVE
ADPVNPEYVV HTLDALLPDD IILAADSGSA ANWYARHLRL RGTMRGSLSG TLATMGPGVP
YVIGAKFAHP GRPALALVGD GAMQMNGMAE LVTAAKYWRE WQDPRLVVAV LNNQDLNQVT
WEMRAMSGAP QFLPSQAIPD VPYADFARSV GLGGVRVEKP DLVEAAWREA LAADRPFVID
FRTDPAVPPI PPHATREQAE AVVSAIVKGD SDRGGMIRQG IKAKVQEFLP GRRQEGNGPG
AQGKR
//
