ID B3QUJ4_CHLT3 Unreviewed; 698 AA.
AC B3QUJ4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Dehydrogenase E1 component {ECO:0000313|EMBL:ACF12900.1};
GN OrderedLocusNames=Ctha_0429 {ECO:0000313|EMBL:ACF12900.1};
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC Chloroherpeton.
OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF12900.1, ECO:0000313|Proteomes:UP000001208};
RN [1] {ECO:0000313|EMBL:ACF12900.1, ECO:0000313|Proteomes:UP000001208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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; CP001100; ACF12900.1; -; Genomic_DNA.
DR RefSeq; WP_012498984.1; NC_011026.1.
DR AlphaFoldDB; B3QUJ4; -.
DR STRING; 517418.Ctha_0429; -.
DR KEGG; cts:Ctha_0429; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000001208; Chromosome.
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 CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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:UP000001208}.
FT DOMAIN 372..548
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 698 AA; 77331 MW; A20C059028BAF50A CRC64;
MMLENVEGLD IKHRNSNGLN HKYNYSVTIS KEQILRAYTQ IYRTRQLDNK LLILLRQGKA
PFHVGAAGHE IAQVAMAMHI KPGQDWSYPY YRDLAYCLEL GMSVEDVVLE FLAKDVSPIS
GGRQMYGHWS HNDLRIPTQS SPTGSQYLHA AGTAIACKRE NELRKEGEKE IVFVSSGEGA
TSEGEFHEAL NWATREKLPV VFLIEDNGYA ISVPIEEQTT GQSIYKVAAG YSGLTRFDVD
GGNFFEMYAA AQKAVDICRR GDGPCLIRAS VVRLLPHSSS DNQAAYRSQD ELESDKKRDG
LLRLEKHILT EGVLSQKELT ALQAEIYNKI EAAVTWALKQ EDPRPESHAD FVVSAEPPPI
SYESTTPQGR SLFMVESINQ ALAEELEHNP KMMVYGEDVG NAKGGVFSAT KGLSEKFGKG
RVFNSQLAEN SIIGTAVGLA FKGYKPVVEI QFGDYIWPGM MQIRNELALI RYRSKGCWSS
PVVVRVAIGG YIHGAMYHSQ NVEGFLAHIP GLFVVYPSNA ADAKGLLKTA CRMDDPVIFL
EHKYLYRQGF AKSPEPDKNY FLPFGKARVV QSGNDATVIT YGATVRLAQE AAAKIQEETN
RTIEILDLRT IIPYDKEAIA ASVKKTGKVL VLHEDTLTQG FGGEIIAFIS ENCFEFLDAP
VYRLGAADTP VPNHPNLELA VLPSKESVYR KLAALVAY
//
