APNO_CUPNN
ID APNO_CUPNN Reviewed; 276 AA.
AC F8GV06;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=CNE_BB1p11570 {ECO:0000312|EMBL:AEI82560.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OG Plasmid pBB1 {ECO:0000312|EMBL:AEI82560.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1;
RX PubMed=21742890; DOI=10.1128/jb.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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).
RN [3] {ECO:0007744|PDB:5T57}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC, AND
RP COFACTOR.
RA Cook W.J., Bonanno J.B., Fedorov E., Huang H., Gerlt J.A., Almo S.C.;
RT "Crystal structure of a semialdehyde dehydrogenase NAD-binding protein from
RT Cupriavidus necator in complex with calcium and NAD.";
RL Submitted (AUG-2016) to the PDB data bank.
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; Evidence={ECO:0000305|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 mM for D-apionate {ECO:0000269|PubMed:29867142};
CC Note=kcat is 0.49 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; CP002879; AEI82560.1; -; Genomic_DNA.
DR RefSeq; WP_013959592.1; NC_015727.1.
DR PDB; 5T57; X-ray; 1.65 A; A=1-276.
DR PDBsum; 5T57; -.
DR AlphaFoldDB; F8GV06; -.
DR SMR; F8GV06; -.
DR EnsemblBacteria; AEI82560; AEI82560; CNE_BB1p11570.
DR KEGG; cnc:CNE_BB1p11570; -.
DR HOGENOM; CLU_087850_0_0_4; -.
DR OMA; VAHPCHP; -.
DR BioCyc; MetaCyc:MON-20970; -.
DR BRENDA; 1.1.1.421; 231.
DR Proteomes; UP000006798; Plasmid pBB1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR031663; PGDH_C.
DR InterPro; IPR037161; Semialdehyde_DH-like_C.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF16896; PGDH_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Metal-binding; NAD;
KW Nucleotide-binding; Oxidoreductase; Plasmid; Zinc.
FT CHAIN 1..276
FT /note="D-apionate oxidoisomerase"
FT /id="PRO_0000446031"
FT BINDING 12..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:5T57"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:5T57"
FT BINDING 69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:5T57"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:5T57"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:5T57"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5T57"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:5T57"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:5T57"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:5T57"
SQ SEQUENCE 276 AA; 30279 MW; 43D836D80492A412 CRC64;
MKEKIALFGA GGKMGVRLAK NLLKSDYRVS HVEVSEVGKK RLKDELGLEC VSTEAALDNV
DVVILAVPDT IIGKIAAQIA PQLRPGTMVM TLDAAAPFAG HLPDRPDLTY FVAHPCHPLI
FNDETDPEAR RDYFGGGAAK QSITSALMQG PEEAFDLGEA VAKVIYAPIL RSYRLTVDQM
ALLEPGLSET ICATLLQVMR EAMDETVRRG VPKEAARDFL LGHMNILGAV IFNEIPGAFS
DACNKAIEFG KPRLMRDDWI KVFDREEIAE SIRRIT
