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Database: UniProt/SWISS-PROT
Entry: APSI_PECAS
LinkDB: APSI_PECAS
Original site: APSI_PECAS 
ID   APSI_PECAS              Reviewed;         332 AA.
AC   Q6D5T7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   13-FEB-2019, entry version 91.
DE   RecName: Full=D-apiose isomerase {ECO:0000303|PubMed:29867142};
DE            EC=5.3.1.- {ECO:0000269|PubMed:29867142};
GN   Name=apsI {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=ECA1953 {ECO:0000312|EMBL:CAG74855.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica and characterization of virulence
RT   factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
RN   [3] {ECO:0000244|PDB:3KTC}
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH IRON.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RG   Joint Center for Structural Genomics (JCSG);
RT   "Crystal structure of putative sugar isomerase (YP_050048.1) from
RT   Erwinia carotovora atroseptica SCRI1043 at 1.54 A resolution.";
RL   Submitted (NOV-2009) to the PDB data bank.
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes
CC       isomerization of D-apiose to apulose.
CC       {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-apiose = apulose; Xref=Rhea:RHEA:56996,
CC         ChEBI:CHEBI:16689, ChEBI:CHEBI:141348;
CC         Evidence={ECO:0000269|PubMed:29867142};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00748};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00748};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
CC       ProRule:PRU00748}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00748}.
DR   EMBL; BX950851; CAG74855.1; -; Genomic_DNA.
DR   RefSeq; WP_011093517.1; NC_004547.2.
DR   PDB; 3KTC; X-ray; 1.54 A; A/B=1-332.
DR   PDBsum; 3KTC; -.
DR   ProteinModelPortal; Q6D5T7; -.
DR   SMR; Q6D5T7; -.
DR   STRING; 218491.ECA1953; -.
DR   DNASU; 2883736; -.
DR   EnsemblBacteria; CAG74855; CAG74855; ECA1953.
DR   KEGG; eca:ECA1953; -.
DR   PATRIC; fig|218491.5.peg.1986; -.
DR   eggNOG; ENOG4107Z96; Bacteria.
DR   eggNOG; COG4952; LUCA.
DR   HOGENOM; HOG000224339; -.
DR   KO; K01805; -.
DR   OMA; YKPNEPR; -.
DR   OrthoDB; 481478at2; -.
DR   BioCyc; PATR218491:G1G3T-2001-MONOMER; -.
DR   EvolutionaryTrace; Q6D5T7; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN         1    332       D-apiose isomerase.
FT                                /FTId=PRO_0000446023.
FT   METAL       166    166       Magnesium 1. {ECO:0000305|Ref.3}.
FT   METAL       201    201       Magnesium 1. {ECO:0000305|Ref.3}.
FT   METAL       204    204       Magnesium 2; via tele nitrogen.
FT                                {ECO:0000305|Ref.3}.
FT   METAL       229    229       Magnesium 1. {ECO:0000305|Ref.3}.
FT   METAL       238    238       Magnesium 2. {ECO:0000305|Ref.3}.
FT   METAL       240    240       Magnesium 2. {ECO:0000305|Ref.3}.
FT   METAL       270    270       Magnesium 1. {ECO:0000305|Ref.3}.
SQ   SEQUENCE   332 AA;  37123 MW;  F14877FC6B01554A CRC64;
     MATYNYPEFG AGLWHFANYI DRYAVDGYGP ALSTIDQINA AKEVGELSYV DLPYPFTPGV
     TLSEVKDALK DAGLKAIGIT PEIYLQKWSR GAFTNPDPAA RAAAFELMHE SAGIVRELGA
     NYVKVWPGQD GWDYPFQVSH KNLWKLAVDG MRDLAGANPD VKFAIEYKPR EPRVKMTWDS
     AARTLLGIED IGLDNVGVLL DFGHALYGGE SPADSAQLII DRGRLFGMDV NDNLRGWDDD
     LVVGTVHMTE IFEFFYVLKI NNWQGVWQLD QFPFRENHVE AAQLSIRFLK HIYRALDKLD
     IPALQAAQEA QNPLQAQRIV QDALLSSITV SE
//
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