ID S3L6F5_TREMA Unreviewed; 818 AA.
AC S3L6F5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=HMPREF9194_00402 {ECO:0000313|EMBL:EPF32404.1};
OS Treponema maltophilum ATCC 51939.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF32404.1, ECO:0000313|Proteomes:UP000014541};
RN [1] {ECO:0000313|EMBL:EPF32404.1, ECO:0000313|Proteomes:UP000014541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF32404.1,
RC ECO:0000313|Proteomes:UP000014541};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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:EPF32404.1}.
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DR EMBL; ATFF01000002; EPF32404.1; -; Genomic_DNA.
DR RefSeq; WP_016524701.1; NZ_KE332518.1.
DR AlphaFoldDB; S3L6F5; -.
DR STRING; 1125699.HMPREF9194_00402; -.
DR PATRIC; fig|1125699.3.peg.406; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_12; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000014541; Unassembled WGS sequence.
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; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000014541}.
FT DOMAIN 472..645
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 818 AA; 90164 MW; 414342CB39EE9B7C CRC64;
MPKSLFVDPK KVRKAEMLKI KDIPVNQYQS DFEKELKTYG AEKLKRILYD MQTIRAFETM
LNTFKTQGAW ENIEYNHKGP AHLSMGQEAA AVGQCVNLGI DDFIFGSHRS HGEILAKCYS
AVEKLSEKEL EKIMKEFLGG DTLKMAEKIS YKNVKDLAEN FVLYGTLAEI FARNAGFNRG
LGGSMHAYFL PFGSMPNNAI VGGSADIATG AALFKRINKK SGIVVSNVGD AALGCGPVWE
AMMMAAMDQY KTLWPESAGG APPILFNFFN NFYGMGGQTC GETMGYGYVA RVGAGVNPQN
MHAERVDGYN PLAVADAIAR KKAILLKGDG PVLLDTITYR VSGHSPSDAS SYRTKEEIDA
WQKADAIEEY KAYLIKNKLI TKADAEKQEN SIREKLIQVV KLATDDKESP RASAAFIESV
MFSNTKADKL ADGKPDVLDV NPETNVRLKA ISGKIRSAFD ADGKPLSKNK MFQYRDGLFE
AMFHRFVTDP TMAAWGEENR DWGGAFAVYR GLTEALPYPR LFNSPISEAA IVGAGVGYAM
SGGRAVVELM YCDFMGRAGD EIFNQASKWQ SMSAGLLKMP LTVRVSVGNK YGAQHSQDWS
ALVAAIPGLK AVFPATPYDA KGMLNYALRG TDPVIFFESQ KLYDKGEEFE KEVPAGYYEI
PEGEPAIRKT GTDITIATLG ATLYTAMNAA KTLKEQYGMD AEIIDIRWIN PLNYEKIVES
VKKTGKLLLV SDAAERGSFM HTVASNMSAL AFDYLDAPVA VLGSRNWITP APECEHYYFP
SVDWILDTIH ERIIPLKGYT PTSVQTTMDI LRKNRQGV
//
