ID A0A136LKS4_9CHLR Unreviewed; 342 AA.
AC A0A136LKS4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component, alpha subunit {ECO:0000313|EMBL:KXK22202.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:KXK22202.1};
GN ORFNames=UZ15_CFX003001103 {ECO:0000313|EMBL:KXK22202.1};
OS Chloroflexi bacterium OLB15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK22202.1, ECO:0000313|Proteomes:UP000070332};
RN [1] {ECO:0000313|EMBL:KXK22202.1, ECO:0000313|Proteomes:UP000070332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB15 {ECO:0000313|EMBL:KXK22202.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KXK22202.1}.
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DR EMBL; LMZS01000054; KXK22202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LKS4; -.
DR STRING; 1617416.UZ15_CFX003001103; -.
DR PATRIC; fig|1617416.3.peg.1155; -.
DR Proteomes; UP000070332; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KXK22202.1}; Pyruvate {ECO:0000313|EMBL:KXK22202.1}.
FT DOMAIN 21..323
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT COILED 284..311
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 342 AA; 37745 MW; FC2B5FD08E9C94CC CRC64;
MATKIESLTK ETLLEWYREI VLIRKFENMC HHLYFEEKDP ARKITGVYLH LATGSEATHV
GAVKALGVDD HVITAYRDHG IAIARGVDPN RVMAEMMGKR TGTSGGKGGS MHLADRSVNF
WGGYAIVGGH VPLGVGIALK EKYVKSGSAV LCFVGDGALN NGYFHEAANM AQVWKLPIVF
LIENNLVGMG TRIEESSGQT NPVKRAAGYG MKEGPSVDGQ NIVEVYEAVK AELDWSRENG
PVLMESRTYR FEGHGVSDKQ FDARDDLKGE LAIWEARDPI NVLADHIKKK YKNIDDELAK
LDTEATQVVN EAVEYAVNSP APDYNDLIAN VYVALTPEYR TR
//