ID V7EDY1_9RHOB Unreviewed; 282 AA.
AC V7EDY1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:ESW59118.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:ESW59118.1};
DE Flags: Fragment;
GN ORFNames=Q27BPR15_19345 {ECO:0000313|EMBL:ESW59118.1};
OS Rhodobacter sp. CACIA14H1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW59118.1, ECO:0000313|Proteomes:UP000018503};
RN [1] {ECO:0000313|EMBL:ESW59118.1, ECO:0000313|Proteomes:UP000018503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24435858;
RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T.,
RA Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a
RT Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium
RT Species.";
RL Genome Announc. 2:e01116-13(2014).
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:ESW59118.1}.
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DR EMBL; AYNO01000223; ESW59118.1; -; Genomic_DNA.
DR AlphaFoldDB; V7EDY1; -.
DR STRING; 1408890.Q27BPR15_19345; -.
DR PATRIC; fig|449393.3.peg.3820; -.
DR Proteomes; UP000018503; Unassembled WGS sequence.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000018503};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ESW59118.1}.
FT DOMAIN 1..141
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESW59118.1"
SQ SEQUENCE 282 AA; 29571 MW; 92190BE8F92B3072 CRC64;
VNTLTKATAP LTAQDFAGRY IHYGVREHGM AAVMNGMALH GGYRPYAGTF LVFADYLHPA
LRLSCLMGLP VTYVLTHDSI GLGEDGPTHQ PVETLAMLRA TPGLVTLRPA DAVEAAEAWE
IALDRAKGPT AIVLSRQDLP VLRADGGVGN ASARGGYVLA EAECGPRRVT IVATGSEVSL
AIEARAVLEA RRIGAAVVSL PSFELFRAQD AAYRAAVLGQ GVRIGVEAAL RFGWDEVIGA
EGGFVGMTGF GASAPAEVLY RHFGITPEAV VALALERLGH DA
//
