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APTA_ACTSZ
ID   APTA_ACTSZ              Reviewed;         276 AA.
AC   A6VKQ4;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Asuc_0171 {ECO:0000312|EMBL:ABR73551.1};
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; ABR73551.1; -; Genomic_DNA.
DR   RefSeq; WP_011978827.1; NC_009655.1.
DR   AlphaFoldDB; A6VKQ4; -.
DR   SMR; A6VKQ4; -.
DR   STRING; 339671.Asuc_0171; -.
DR   EnsemblBacteria; ABR73551; ABR73551; Asuc_0171.
DR   KEGG; asu:Asuc_0171; -.
DR   eggNOG; COG3959; Bacteria.
DR   HOGENOM; CLU_009227_4_1_6; -.
DR   OMA; MVHAVNS; -.
DR   OrthoDB; 1543182at2; -.
DR   BioCyc; MetaCyc:MON-20956; -.
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   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..276
FT                   /note="Apulose-4-phosphate transketolase subunit A"
FT                   /id="PRO_0000446025"
SQ   SEQUENCE   276 AA;  30173 MW;  A54FF3A4C84494EC CRC64;
     MNPYNLSYDE LEKKAKAIRR KIVVLNANSP AGGHTGADLS QVEILTSLYF RVLNNDPKDL
     INPERDIYIQ SKGHGAGGYY CCLAEAGYIP EDWLPTYQHS DSKLPGHPVK HKTPGVELNT
     GALGHGLPVA VGLAIAAKKS GSKRKIYVLT GDGELGEGSN WEAALTAAQY KLDNLIIIND
     KNKLQLAGFT KDILCTDPLD KKWEAFGMEV HECQGNDIRS VVDTLESIQP NGKPHVVIAN
     TTKGAGISFI EGRPEWHHKV PKGDEVELAL EELKDE
 
 
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