APNO_AGRRK
ID APNO_AGRRK Reviewed; 275 AA.
AC B9JK75;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Arad_9232 {ECO:0000312|EMBL:ACM30317.1};
OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=311403;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K84 / ATCC BAA-868;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(2009).
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=0.15 mM for D-apionate {ECO:0000269|PubMed:29867142};
CC Note=kcat is 1.3 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; CP000629; ACM30317.1; -; Genomic_DNA.
DR RefSeq; WP_015917645.1; NC_011983.1.
DR AlphaFoldDB; B9JK75; -.
DR SMR; B9JK75; -.
DR STRING; 311403.Arad_9232; -.
DR EnsemblBacteria; ACM30317; ACM30317; Arad_9232.
DR KEGG; ara:Arad_9232; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_087850_0_0_5; -.
DR OMA; VAHPCHP; -.
DR OrthoDB; 690763at2; -.
DR BioCyc; MetaCyc:MON-20960; -.
DR BRENDA; 1.1.1.421; 200.
DR Proteomes; UP000001600; Chromosome 2.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR019665; OxRdtase/DH_put_Rossmann_dom.
DR InterPro; IPR031663; PGDH_C.
DR InterPro; IPR037161; Semialdehyde_DH-like_C.
DR Pfam; PF16896; PGDH_C; 1.
DR Pfam; PF10727; Rossmann-like; 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..275
FT /note="D-apionate oxidoisomerase"
FT /id="PRO_0000446029"
FT BINDING 11..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:F8GV06"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:F8GV06"
FT BINDING 68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:F8GV06"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:F8GV06"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:F8GV06"
SQ SEQUENCE 275 AA; 29724 MW; 3266E09D69ECD7D6 CRC64;
MTVIALFGAG GKMGYRLAKN LKGSRFDVRH VEVSDAGKAR LKNDLDLSCV PVDEALNGAE
VVILAVPDTA IGKVAAGIVD KLKPGTMVVA LDAAAPFAGH LPKRDELTYF VTHPCHPPIF
NDETDMQAKK DHFGGLFAKQ HIVSALMQGP ESAYALGEEI AKVIWAPVMR SHRVTVEQMA
MLEPGLSETV CASLLVVMRQ AMDECVARGV PEDAARDFLL GHMNVLGAVI FKEVDGVFSD
ACNKAIEFGI PALMRDDWKN VFEPKEIAAS IQRIT
