ID S4H343_GARVA Unreviewed; 265 AA.
AC S4H343;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Transketolase, pyridine binding domain protein {ECO:0000313|EMBL:EPI57741.1};
DE Flags: Fragment;
GN ORFNames=HMPREF1572_00376 {ECO:0000313|EMBL:EPI57741.1};
OS Gardnerella vaginalis JCP7275.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1261057 {ECO:0000313|EMBL:EPI57741.1, ECO:0000313|Proteomes:UP000014557};
RN [1] {ECO:0000313|EMBL:EPI57741.1, ECO:0000313|Proteomes:UP000014557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCP7275 {ECO:0000313|EMBL:EPI57741.1,
RC ECO:0000313|Proteomes:UP000014557};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-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:EPI57741.1}.
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DR EMBL; ATJS01000014; EPI57741.1; -; Genomic_DNA.
DR AlphaFoldDB; S4H343; -.
DR PATRIC; fig|1261057.4.peg.353; -.
DR HOGENOM; CLU_009227_2_0_11; -.
DR Proteomes; UP000014557; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 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); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 4: Predicted;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..121
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPI57741.1"
SQ SEQUENCE 265 AA; 29099 MW; 3837DD0F1AE1C1C5 CRC64;
HFGVREFAMG AITNGILLGS DTRPFNGTFF QFSDYERPAV RLAALMEIPN LYVWTHDSVA
LGEDGPTHQP IEHLAAFRAI PQLEVVRPAD EYETAEAYRY FFEKKNNYPT AMILTRQGVP
TLAETAEKAR EGVKHGGYVL VDCEGTPDVI IMATGSEVQW AVAGAKTLAA EGIKARVLSM
PSLEWFEEQD EEYKEAILPK SVKARVSIEA GLALPWYKYL GDCGKAVSIE QYGLQGDGGQ
NMIDLGITAE HVVEAAKASI EEARA
//
