ID   APNO_PECAS              Reviewed;         285 AA.
AC   Q6D8V3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=D-apionate oxidoisomerase {ECO:0000303|PubMed:29867142};
DE            EC=1.1.1.421 {ECO:0000269|PubMed:29867142};
GN   Name=apnO {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=ECA0869 {ECO:0000312|EMBL:CAG73781.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, 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).
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the conversion
CC       of D-apionate to 3-oxo-isoapionate. {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-apionate + NAD(+) = 3-oxoisoapionate + H(+) + NADH;
CC         Xref=Rhea:RHEA:57044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:141352, ChEBI:CHEBI:141353;
CC         EC=1.1.1.421; Evidence={ECO:0000269|PubMed:29867142};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:F8GV06};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 mM for D-apiose {ECO:0000269|PubMed:29867142};
CC         Note=kcat is 0.47 sec(-1). {ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the ApnO family. {ECO:0000305}.
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DR   EMBL; BX950851; CAG73781.1; -; Genomic_DNA.
DR   RefSeq; WP_011092472.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8V3; -.
DR   SMR; Q6D8V3; -.
DR   STRING; 218491.ECA0869; -.
DR   DNASU; 2881392; -.
DR   EnsemblBacteria; CAG73781; CAG73781; ECA0869.
DR   GeneID; 57207612; -.
DR   KEGG; eca:ECA0869; -.
DR   PATRIC; fig|218491.5.peg.869; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_087850_0_0_6; -.
DR   OMA; VAHPCHP; -.
DR   OrthoDB; 690763at2; -.
DR   BioCyc; MetaCyc:MON-20972; -.
DR   BRENDA; 1.1.1.421; 9330.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3640.10; -; 1.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR031663; PGDH_C.
DR   InterPro; IPR037161; Semialdehyde_DH-like_C.
DR   Pfam; PF07991; IlvN; 1.
DR   Pfam; PF16896; PGDH_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Metal-binding; NAD; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..285
FT                   /note="D-apionate oxidoisomerase"
FT                   /id="PRO_0000446032"
FT   BINDING         15..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:F8GV06"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:F8GV06"
FT   BINDING         71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:F8GV06"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:F8GV06"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:F8GV06"
SQ   SEQUENCE   285 AA;  30932 MW;  02175B135A89BF06 CRC64;
     MAAELKTITV LGAGGKMGMR ISANFQKSDY QVFYCENSPR AQEQVVAAGR ELSIAEQVIP
     ESDVVILAVP DIALKAVSGI VVPQMKSNAV LLTLDPAAAY ANLIAKRDDI DYAVAHPCHP
     SVFLDRFTPE EHADAFGGVA APQHVAASYE TGSDEQKATL ARVVKVMYGP VIDVHWVTVK
     QLAYLEPTLV ETVACMVGTL MKEALDETIN TIGVPEAAAK AMLYGHIQIA LAVAFRSTNP
     FSDACMIAIE YGKENIIKPD WKKIFDEKEL DLVIAKMLKI DAIER