ID G0IW72_CYCMS Unreviewed; 806 AA.
AC G0IW72;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Transketolase domain-containing protein {ECO:0000313|EMBL:AEL26292.1};
GN OrderedLocusNames=Cycma_2553 {ECO:0000313|EMBL:AEL26292.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL26292.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) 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; CP002955; AEL26292.1; -; Genomic_DNA.
DR RefSeq; WP_014020585.1; NC_015914.1.
DR AlphaFoldDB; G0IW72; -.
DR STRING; 880070.Cycma_2553; -.
DR KEGG; cmr:Cycma_2553; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_350462_0_0_10; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000001635; 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 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:UP000001635}.
FT DOMAIN 472..646
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 806 AA; 90350 MW; C1597A25AAF5AE92 CRC64;
MNTEYLPTLT KENASILDVQ SVLNDYRMVM ISRHASLTVR KEVFMGKAKF GVYGDGKELA
QVAMAKFFRM GDFRSGYYRD QTLLFAMEEL SIQEYFAQLY AHTDINAEPA SGGRLMNAHF
ATRSLNEDGS WKNLMKMKNS TADISPTAAQ MPKLLGLAYA SKLYRENTAL HDMTTFSNKG
NEVAWGTIGN ASTAEGMFFE TFNAGGVLQV PMVISVWDDE YGISVTNDLQ ITKSSISAVL
EGFKRDNQEK GYEILVVNGW DYKGLVNAYG RANKLAREKH IPVLVHVQGM TQPQGHSTSG
SHERYKSKER LAWEAEHDCV VKFKEYILEN KIASEEELDQ IDSEAKKLVK ESKDKAWKAF
TATIRTELEE AVVLLNDLAK KIKNSSELIR MAGELKRTLN PVRMDVISTV RKALLLVRNE
PLEVKLRLQS WYRTQQELNE DRYSSHQYSE SAFRVEAIAP VEVSYPEKPE LLDGREVLKA
CFDAILSRDP RVFVIGEDVG QIGDVNQAFA GLQAKHGSLR VTDTGIREVT IIGQGIGAAL
RGLRPITEVQ YLDYLIYALM TLSDDLACLH YRTKGGQKAP LIIRTRGHRL EGVWHSGSPI
SMILGSLRGI LLCVPRNMTQ AAGMYNTLLE ADQPAIVIES LNGYRLKEKM PSNIGTFKVA
LGKAEVLQEG KDITVVTYGS MCRIVMDAAK QLFNIGIYVE VIDVQTLVPF DLDEVILNSI
KKTNRVIFAD EDVPGGASAY MMQQVLEKQN AYYYLDAQPI TLSAKEHRPA YSSDGDYFSK
PSVDDVVEKV YSVMNEADPK KFPEIY
//
