ID D9X142_STRVT Unreviewed; 400 AA.
AC D9X142;
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 (Acetyl-transferring) E1 component, alpha subunit {ECO:0000313|EMBL:EFL33480.1};
GN ORFNames=SSQG_03998 {ECO:0000313|EMBL:EFL33480.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL33480.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
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 viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; GG657757; EFL33480.1; -; Genomic_DNA.
DR RefSeq; WP_003991588.1; NZ_GG657757.1.
DR AlphaFoldDB; D9X142; -.
DR STRING; 591159.SSQG_03998; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:EFL33480.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT DOMAIN 78..359
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43834 MW; 47C913F3C0B71D94 CRC64;
MTVESTAART SRRSAGSKAG TTGTKRTTRT TAKKDAGAKG TEPQLVQLLT PEGKRVKNAE
YDKYVAGVTP EELRGLYRDM VLTRRFDAEA TALQRQGELG LWASLLGQEA AQIGSGRATR
EDDYVFPTYR EHGVAWCRGV DPTNLLGMFR GVNNGGWDPN SNNFQLYTIV IGSQTLHATG
YAMGVAKDGA DSAVIAYFGD GASSQGDVAE SFTFSAVYNA PVVFFCQNNQ WAISEPTEKQ
SRVPIYQRAQ GFGFPGVRVD GNDVLGVLAV TRWALERARS GEGPTLVEAF TYRMGAHTTS
DDPSRYRGDE ERQAWEAKDP ILRLRRYLEA SNHADEGFFA ELEAESEALG KRVREAVRAM
PDPDRFAIFE NVYADGHALV DEERAQFAAY QASFADEGGN
//
