APTA_PHOV8
ID APTA_PHOV8 Reviewed; 281 AA.
AC A6KXB4;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Apulose-4-phosphate transketolase subunit A {ECO:0000305};
DE EC=2.2.1.13 {ECO:0000269|PubMed:29867142};
DE AltName: Full=Apulose-4-phosphate transketolase N-terminal subunit {ECO:0000305};
GN Name=aptA {ECO:0000305|PubMed:29867142};
GN OrderedLocusNames=BVU_0359 {ECO:0000312|EMBL:ABR38078.1};
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA Andersen H.M., Almo S.C., Gerlt J.A.;
RT "Functional assignment of multiple catabolic pathways for D-apiose.";
RL Nat. Chem. Biol. 14:696-705(2018).
CC -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the transfer of
CC the glycolaldehyde group from apulose-4-phosphate to D-glyceraldehyde
CC 3-phosphate, generating dihydroxyacetone phosphate and D-xylulose-5-
CC phosphate. {ECO:0000269|PubMed:29867142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apulose 4-phosphate + D-glyceraldehyde 3-phosphate = D-
CC xylulose 5-phosphate + dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:57024, ChEBI:CHEBI:57642, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:59776, ChEBI:CHEBI:141351; EC=2.2.1.13;
CC Evidence={ECO:0000269|PubMed:29867142};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P29401};
CC -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC -!- SUBUNIT: Probable heterodimer composed of AptA and AptB.
CC {ECO:0000305|PubMed:29867142}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; CP000139; ABR38078.1; -; Genomic_DNA.
DR RefSeq; WP_011964721.1; NC_009614.1.
DR AlphaFoldDB; A6KXB4; -.
DR SMR; A6KXB4; -.
DR STRING; 435590.BVU_0359; -.
DR EnsemblBacteria; ABR38078; ABR38078; BVU_0359.
DR KEGG; bvu:BVU_0359; -.
DR PATRIC; fig|435590.9.peg.371; -.
DR eggNOG; COG3959; Bacteria.
DR HOGENOM; CLU_009227_4_1_10; -.
DR OMA; GQGYIAQ; -.
DR OrthoDB; 1543182at2; -.
DR BioCyc; BVUL435590:G1G59-378-MON; -.
DR BRENDA; 2.2.1.13; 776.
DR Proteomes; UP000002861; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02012; TPP_TK; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Reference proteome; Thiamine pyrophosphate;
KW Transferase.
FT CHAIN 1..281
FT /note="Apulose-4-phosphate transketolase subunit A"
FT /id="PRO_0000446026"
SQ SEQUENCE 281 AA; 31468 MW; 9979AF79B9CF5103 CRC64;
MQVETLELQS EKNRKRLVEI VYKAKAGHIG GDLSCLNVLT ALYFDIMRVW PDKPKETKRD
RFVMSKGHCV EALYVTLEAK GFISREVTDT LGEFGSILSG HPTIEVPGIE VNTGALGHGL
SVGVGMAMAA KMDKADYKTY VLMGDGEQGE GSIYEAAMAG NQYKLDNLVA IIDRNRLQIS
GTTEEVMSLE SMRDRWTAFG WDVLEMNGDE MEDIIRTFRS IDYTNKKPHL LISHTTKGKG
VSYMEGIAKW HHGVPTAEQY EEAVREVSER IEKLEKENNG K