ID W0J9W7_9BACT Unreviewed; 681 AA.
AC W0J9W7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AHF93479.1};
GN ORFNames=OPIT5_28055 {ECO:0000313|EMBL:AHF93479.1};
OS Opitutaceae bacterium TAV5.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF93479.1, ECO:0000313|Proteomes:UP000003813};
RN [1] {ECO:0000313|EMBL:AHF93479.1, ECO:0000313|Proteomes:UP000003813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF93479.1};
RX PubMed=25744998;
RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA Rodrigues J.L.;
RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT Potential Facultative Methylotroph of the Wood-Feeding Termite
RT Reticulitermes flavipes.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP007053; AHF93479.1; -; Genomic_DNA.
DR AlphaFoldDB; W0J9W7; -.
DR STRING; 794903.OPIT5_28055; -.
DR KEGG; obt:OPIT5_28055; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_2_1_0; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000003813; 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:UP000003813}.
FT DOMAIN 361..534
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 681 AA; 74587 MW; 4465C534DEA98CE6 CRC64;
MAFPQIPAIL AERDISTSDL NTPPALVRLY AWMFYARVTD DRIVDLFRQG LIKGTAAGGQ
GNEGLIIPLA LLADKAIDVI SFTHRDLGGH LIWSGHLCEH LDQYFANSQS PTRAREGNVH
HGDPANRSLP MISHLGSMIS NVAGLADAQR RAGKPAVGFA LFGDGGSSTG DIHETLNLAS
LLSLPVVFIV ENNDIAYSTP VSEQYPAGVE LWTRAAAYNM EGRFLDATDD PEKIARQLAD
AIDTVRSTSR PLLIEARTLR LRGHAAYDTR DYLSAGQIQA IDAADPLPRF RTRLVAEGHA
ALIEKHEQDI RVFIEDCIKV SLAVPPPSPS SLPPDAFAPS TTEIAWKPDL GPGSAGAPEP
LTLAQAINRG LRKILAERPE SLLLGQDIGV YGGAFKVTEH LLRDFGRARV FNTPLAESAC
TGYATGLALG GIRTIEEFQF ADFSTEAVTQ ITQNAATYHY RSGAKVPMVF RFPCGGGITV
GSFHSQELET LFLAFPGIKA LYPSTPQDAF NALLAAYEDD NPVCLFEHKG LYRRGKHPVS
WDPAWRDVWQ PRHVRAGDFA TLVTYGEMVH HATEAASYLE NEYERTIDLF DLRALSPLRL
EQIEASLART HRLIVIHEGH RTHGFGAELV ARLTEKHFFD LEAPPLRIAS LDIPVPFAPE
LEAVYRPARD SIIGKIVAWL G
//
