ID A0A1G5S3R7_9FIRM Unreviewed; 663 AA.
AC A0A1G5S3R7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN03080599_02457 {ECO:0000313|EMBL:SCZ80808.1};
OS Acidaminobacter hydrogenoformans DSM 2784.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Acidaminobacter.
OX NCBI_TaxID=1120920 {ECO:0000313|EMBL:SCZ80808.1, ECO:0000313|Proteomes:UP000199208};
RN [1] {ECO:0000313|EMBL:SCZ80808.1, ECO:0000313|Proteomes:UP000199208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2784 {ECO:0000313|EMBL:SCZ80808.1,
RC ECO:0000313|Proteomes:UP000199208};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; FMWL01000014; SCZ80808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5S3R7; -.
DR STRING; 1120920.SAMN03080599_02457; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000199208; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
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 Pfam; PF00456; Transketolase_N; 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.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199208};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 354..525
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 663 AA; 72612 MW; 1AF140E65860723E CRC64;
MYAMDHEVIK TIRLLSADAV EKANSGHPGL PMGAAAMAFV LWKDFLKGSA TDPHWADRDR
FVLSAGHGSA LLYSLLHLFG YEVTLEDLKK FRQVGSLTPG HPEFDVTPGV ETTTGPLGQG
FGNAVGMAIA EMRLAEEFNT QDFNLVDHYT YVLAGDGDLM EGVSAESASL AGHLKLGKLI
VLYDDNGITI DGGTEISFTE DVLKRFEAYG WQVSRVEDGN DLKAIHDALH AAKLDTSKPS
LIAVRTTIGY GSPNKAGKSA AHGAPLGPDE LAMTKVHMEA DPEAFFQVSE EVCAYMDEII
DRREIDRFMW EEKVEAYILK YPEKAEAWKR WFDYELMQDN FDTEAFYKRF DKADATRSHG
GEAMNALIEL APNFMGGSAD LNSSTKTLLK GKGDFGRMQR GGANINFGVR EHAMASILNG
MALHGGLRVF GSTFLVFADY MKPALRLSAL MGLPVVYVFT HDSIAVGEDG PTHQPIEHLL
MLRSIPNMFV YRPADGIETA ASWIEILKRV EGPSALILTR QKVGSLGVRE MQVDRGAYVV
LPEMGAQPEV ILMATGSEVE LAVAAAEKLR AAGKDPRVVS IPCVEQFLEQ SPAYIEMILP
KAVEKRVSIE MGRTLGWERF VGLNGMSIGI DRFGESGPGE VVMAHFGFTP EKVSDRILAY
LAK
//
