ID A7IFJ0_XANP2 Unreviewed; 692 AA.
AC A7IFJ0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN OrderedLocusNames=Xaut_1535 {ECO:0000313|EMBL:ABS66783.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS66783.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS66783.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS66783.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IFJ0; -.
DR STRING; 78245.Xaut_1535; -.
DR KEGG; xau:Xaut_1535; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_5; -.
DR OrthoDB; 8732661at2; -.
DR PhylomeDB; A7IFJ0; -.
DR Proteomes; UP000002417; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002417}.
FT DOMAIN 385..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 692 AA; 73247 MW; DC18FB9CCD2E438B CRC64;
MSLIASTGFA EAGNALARPN SGDGTPSARL NSGDGFASAR RMADAIRFLA LDAIAKAEDG
HPGAPLGGAE LATALFTRHF KCNPADPAWF DRDRFVLSNG HGSMLIYAVL HLAGYAGMPM
EEIRRFRELG AHTHGHPERD VALGIEVTTG PLGQGIANAV GMAVAEAFLS ATYGPELVDH
RTYAVVGDGC LMEGIAHEVI SLAGHLKLGK LTFLWDDNRM TDDGGTHFAI SEDVRARFRI
AGWQVIDADG HDVEAVSAAL ILAHQDPRPT MIACTTVLGK GLPRLEGKRG AHGGRVFPED
VVEARAAAGW THGPFEVPQD VAAAWQAGTG ERNRPSYEAW QARVAALPAD KRAEFERLVR
GELPAGVLSA LSAHAEALAA AAPAQSSNQS TADIVDLLAG LVPELLPGAP DLEGPTNCKR
GLDAFTAENP AGRYIHYGIR EHAMGSMMNG MVAHGGVLPL GATYLVFSDY MRPSLRMSAL
MELPVITLYS HDSIGIGKNG PTHQPVEFLA SLRAMPNMAV FRPADAVETA ECWQLALARR
DGPSSIICSR QALPAQRSDA GENRSARGAY VLRAAEGGPR RVTLIATGSE VDVAVKARDL
LQAEGIPTAV VSMPCWEIFG EQDEAYVWEV LGPGTVRVAV EAAVKLGWER WIGADGAFVG
MNSFGASGPA DELFRHFGIT PAAVGDAARA RL
//