APNO_BLAHS
ID APNO_BLAHS Reviewed; 287 AA.
AC C0CMQ7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
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 ORFNames=RUMHYD_02142 {ECO:0000312|EMBL:EEG48952.1};
OS Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33)
OS (Ruminococcus hydrogenotrophicus).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=476272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10507 / JCM 14656 / S5a33;
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10507 / JCM 14656 / S5a33;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Blautia hydrogenotrophica DSM 10507 (Ruminococcus
RT hydrogenotrophicus DSM 10507).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
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=0.25 mM for D-apionate {ECO:0000269|PubMed:29867142};
CC Note=kcat is 0.32 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; ACBZ01000114; EEG48952.1; -; Genomic_DNA.
DR RefSeq; WP_005949243.1; NZ_GG657685.1.
DR AlphaFoldDB; C0CMQ7; -.
DR SMR; C0CMQ7; -.
DR STRING; 476272.RUMHYD_02142; -.
DR EnsemblBacteria; EEG48952; EEG48952; RUMHYD_02142.
DR PATRIC; fig|476272.21.peg.1574; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_087850_0_0_9; -.
DR OrthoDB; 690763at2; -.
DR BRENDA; 1.1.1.421; 17157.
DR Proteomes; UP000003100; Unassembled WGS sequence.
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; Zinc.
FT CHAIN 1..287
FT /note="D-apionate oxidoisomerase"
FT /id="PRO_0000446030"
FT BINDING 13..15
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 287 AA; 31231 MW; 6339EBB154AF8B8F CRC64;
MGKIVVSVIG AGGKMGTRTS NNLAKKPEEF DLLLVEASEA GIQSIKDRGF EPTPVEEALE
KSDVVVFAVP DTLIGKLSAI YVPQLKPGTG FIILDPAAAV ARELTLRDDC TFGVAHPCHP
SYFLDQDTYE ARQDRFGGCG GKQDIVMSKI QGNDDRFAQC VEVAKQMYAP VEHAYVMSSE
QIAFLEPTLV ELLGATCLYA MAETVDEAVK RGIPKEAAVS FLTGHIYNLS ANFLGYIPGN
PPVSDACKVA IGLGNRLVMR EDWKKIWDDE VLNKVIATML HPDKPQI
