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 03-AUG-2022, entry version 104.
DE RecName: Full=D-apiose isomerase {ECO:0000303|PubMed:29867142};
DE EC=5.3.1.36 {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 carotovora
RT subsp. atroseptica and characterization of virulence 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:0007744|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 Erwinia
RT 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 isomerization
CC of D-apiose to apulose. {ECO:0000269|PubMed:29867142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-apiose = apulose; Xref=Rhea:RHEA:56996,
CC ChEBI:CHEBI:16689, ChEBI:CHEBI:141348; EC=5.3.1.36;
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-ProRule:PRU00748}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00748}.
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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 AlphaFoldDB; 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; COG1082; Bacteria.
DR HOGENOM; CLU_072264_0_0_6; -.
DR OMA; MGQDGFD; -.
DR OrthoDB; 481478at2; -.
DR BioCyc; MetaCyc:MON-20954; -.
DR BRENDA; 5.3.1.36; 9330.
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; Cytoplasm; Isomerase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..332
FT /note="D-apiose isomerase"
FT /id="PRO_0000446023"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:3KTC"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 278..298
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:3KTC"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:3KTC"
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
