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