ID A0A0C1L0S7_9BACT Unreviewed; 797 AA.
AC A0A0C1L0S7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KIC93196.1};
GN ORFNames=OI18_18225 {ECO:0000313|EMBL:KIC93196.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC93196.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC93196.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC93196.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) 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:KIC93196.1}.
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DR EMBL; JSVC01000021; KIC93196.1; -; Genomic_DNA.
DR RefSeq; WP_039142446.1; NZ_JSVC01000021.1.
DR AlphaFoldDB; A0A0C1L0S7; -.
DR STRING; 1349421.OI18_18225; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000031408; 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; 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:UP000031408}.
FT DOMAIN 473..647
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 797 AA; 89794 MW; 1A0FD6A6D5929321 CRC64;
MEKLMDQDLI ASEKLSFDHF REEVLRDYQL ACESREASLM GRKEVLTGKA KFGIFGDGKE
VAQIAAAKFF RPGDFRAGYY RDQTFVFASK LATVEQFFAQ LYANPDINQD PFSAGRQMNS
HFATPNVDEE GNWMPLAYQK NVSSDMAPTA GQMPRALGLA YASKVFRNVD GLKDFPELSN
NGNEVCFCTI GDASTSEGHF WEAVNAAGVM QVPLAIFVWD DGYGISVPKK YQTTKGSISE
VLKGFQQRDG SNGLDIYRLK GWDYAGMVEV MEPAIQKIRD THIPAVFHVE EITQPQGHST
SGSHERYKSP ERLEWERAFD CIKKFREWIL ENVLSSEEEL NDLEIRAKEN VRDAKNRAWS
IYLQPIKDQV TRVLELTRNV VPQVPEKAAR LNELVTRLEA EKEPMRRDVM HTLHQVIETL
GRHDSAFWLK DYYRELKELN ASLYNTHLYN EGPKSALNVT PVPVTYSADA PMLNGYEVLN
RYFDQLFTTN PKVIAFGEDV GYIGDVNQGF AGLQAKHGEF RISDTGIREL TIMGQGVGAA
FRGLRPIAEI QYLDYLLYGL QPLSDDVATT HYRTSGKQSC PLIVRTRGHR LEGIWHSGSP
MGMIINSLRG MYVCVPRNMV QAVGMYNTLL KANDPAIMIE CLNGYRLKEK MPDNLNEFTL
PLGIPEVLRS GSDITIVSYG ATLRIVQEAA NMLAESGVQC EIVDVQTLLP FDINHKILES
LKKTNRILFA DEDVPGGAAA YMFNHVMEVQ GGYRWLDVAP RTLTAKAHRP AYASDGDYFS
KPNVEDVFEV VKEMMAE
//
