ID   APTB_ACTSZ              Reviewed;         311 AA.
AC   A6VKQ3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Apulose-4-phosphate transketolase subunit B {ECO:0000305};
DE            EC=2.2.1.13 {ECO:0000269|PubMed:29867142};
DE   AltName: Full=Apulose-4-phosphate transketolase C-terminal subunit {ECO:0000305};
GN   Name=aptB {ECO:0000305|PubMed:29867142};
GN   OrderedLocusNames=Asuc_0170 {ECO:0000312|EMBL:ABR73550.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR73550.1; -; Genomic_DNA.
DR   RefSeq; WP_011978826.1; NC_009655.1.
DR   AlphaFoldDB; A6VKQ3; -.
DR   SMR; A6VKQ3; -.
DR   STRING; 339671.Asuc_0170; -.
DR   EnsemblBacteria; ABR73550; ABR73550; Asuc_0170.
DR   KEGG; asu:Asuc_0170; -.
DR   eggNOG; COG3958; Bacteria.
DR   HOGENOM; CLU_009227_1_1_6; -.
DR   OMA; KVDVCYN; -.
DR   OrthoDB; 900125at2; -.
DR   BioCyc; MetaCyc:MON-20957; -.
DR   BRENDA; 2.2.1.13; 8032.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Reference proteome; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..311
FT                   /note="Apulose-4-phosphate transketolase subunit B"
FT                   /id="PRO_0000446027"
SQ   SEQUENCE   311 AA;  33097 MW;  208A1DEE3EA98BA8 CRC64;
     MSNAEHLANI MVERFISAVK NGVDLVPVVA DSTSTAKIAP FIKEFPDRLV NVGIAEQSLV
     GCAAGLALGG KVAVTCNAAP FLISRANEQV KVDVCYNNTN VKLFGLNSGA SYGPLASTHH
     SIDDIGVMRG FGNIQIFAPS SPNECRQIID YAINYVGPVY IRLDGKELPE IHNDDYEFVP
     GQIDVLRKGG KIALVAMGST VYEIVDAAVK LAEKGIEVTV VNVPSIRPCD TEALFNAIKD
     CKYVISVEEH NINGGVGSLV AEVIAEHGAP ITLKRRGIAD GGYALAGDRK SMRKHHGIDA
     DSIVDLALSL N