ID A0A292RCN3_9BACT Unreviewed; 319 AA.
AC A0A292RCN3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:DAA95268.1};
GN ORFNames=CPT80_08115 {ECO:0000313|EMBL:DAA95268.1};
OS Candidatus Gastranaerophilales bacterium HUM_9.
OC Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA95268.1, ECO:0000313|Proteomes:UP000218540};
RN [1] {ECO:0000313|EMBL:DAA95268.1, ECO:0000313|Proteomes:UP000218540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUM_9 {ECO:0000313|EMBL:DAA95268.1};
RX PubMed=28360330; DOI=.1126/science.aal3794;
RA Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT "On the origins of oxygenic photosynthesis and aerobic respiration in
RT Cyanobacteria.";
RL Science 355:1436-1440(2017).
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:DAA95268.1}.
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DR EMBL; DABG01000019; DAA95268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292RCN3; -.
DR STRING; 1916320.GCA_002103075_00761; -.
DR Proteomes; UP000218540; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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 8..174
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 319 AA; 34729 MW; 860DD4D470AF670E CRC64;
MIDVSKKRST REAFGKALVE LGKENEKVVV LDADLSVSTQ TKLFAKEFPD RFFDIGIAEQ
DLIGTAAGLA AVGKIPYTAT FAVFATGRTY DQIRNTVCYS NFNVKIVGTH GGITVGEDGA
THQALEDIAL MANLPNMTVI VPSDYAETFS AIKYASTINT PVYIRVARAN LPDVFEDGYK
ISPKAKLMRE GKDLTIVTNG ETLQESLIAV EELAKKGIDV ELLHIPFVKP FDKESVIKSA
KKTNLVVTIE NHSIKGGLGS AVCETLSEVY PTKVIRMGID DEFGMSGTAK ELMAHFKLDS
NSIVERIVEI KNDTIKSGN
//
