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Entry: A0A0F5IUU2_9BACT
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ID   A0A0F5IUU2_9BACT        Unreviewed;       676 AA.
AC   A0A0F5IUU2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=HMPREF1536_04388 {ECO:0000313|EMBL:KKB49324.1};
OS   Parabacteroides gordonii MS-1 = DSM 23371.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB49324.1, ECO:0000313|Proteomes:UP000033035};
RN   [1] {ECO:0000313|EMBL:KKB49324.1, ECO:0000313|Proteomes:UP000033035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-1 {ECO:0000313|EMBL:KKB49324.1,
RC   ECO:0000313|Proteomes:UP000033035};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA   Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL   Submitted (APR-2013) 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:KKB49324.1}.
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DR   EMBL; AQHW01000025; KKB49324.1; -; Genomic_DNA.
DR   RefSeq; WP_028729118.1; NZ_KQ033920.1.
DR   AlphaFoldDB; A0A0F5IUU2; -.
DR   STRING; 1203610.HMPREF1536_04388; -.
DR   PATRIC; fig|1203610.3.peg.4469; -.
DR   HOGENOM; CLU_012907_2_1_10; -.
DR   Proteomes; UP000033035; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033035}.
FT   DOMAIN          348..527
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   COILED          279..310
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   676 AA;  75682 MW;  821D68FC1B8762A9 CRC64;
     MKKYDIKNTD KETLKKWFYL MTLGRALDEK APSYLLQSLG WSYHAPYAGH DGIQLAIGQV
     FKKGEDFLFP YYRDMLTVLS AGMTPEEIIL NGISKATDLT SAGRHMSNHF SKMEWNIENI
     SSATGTHDLH AAGVGRAMVY YKHKGVAITS HGESATSEGF VYEAINGAST ERLPVIFVIQ
     DNGYGISVPK EDQTANRKVA DNFSGFKNLK IIHCNGKDVF DSMNAMTEAK EYALNRIPVI
     VQANCVRIGS HSNSDKHTLY RDENELNYVK AADPLQKFRR MLLRYKRFTE EELKEIEEKA
     KKDLSAANRK ALAAPDPDPA TVTDFVLPEP YIPKKYIDGV QNEAGEKETL ATAINKTLKA
     EFRHNPDTFI WGQDIANKDK GGVFNISKGM QQEFGDTRVF NAPIAEDYIV GSANGMCRFD
     PKIHVVIEGA EFADYFWPAV EQYVECTHEY WRSYGQFTPN ITLRLASGGY IGGGLYHSQT
     IEGALTTLPG ARIVYPSFAD DAAGLLRTSM RSKGFTLFLE PKALYNATEA ATVVPDDFEV
     PFGKARIRRP GEDMSIITYG NTTHLCLNVA ERLQKEHDRN VEVIDIRSLI PLDKDTIFES
     VKKTSKVLIV HEDKVFSGFG AEIASIIGSE LFRYLDAPIQ RVGSIFTPVG FHPVLEKAIL
     PDEEKIYKAA KELLDY
//
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