CARDI_NOVAD
ID CARDI_NOVAD Reviewed; 469 AA.
AC A4XES9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=8'-apo-carotenoid 13,14-cleaving dioxygenase {ECO:0000305};
DE EC=1.13.11.82 {ECO:0000269|PubMed:22711425};
DE AltName: Full=NACOX1 {ECO:0000303|PubMed:22711425};
GN OrderedLocusNames=Saro_3580 {ECO:0000312|EMBL:ABP64440.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL2 {ECO:0000312|EMBL:ABP64440.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF HIS-170; HIS-219; HIS-284 AND HIS-460.
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RX PubMed=22711425; DOI=10.1007/s10529-012-0969-5;
RA Kim Y.S., Seo E.S., Oh D.K.;
RT "Characterization of an apo-carotenoid 13,14-dioxygenase from
RT Novosphingobium aromaticivorans that converts beta-apo-8'-carotenal to
RT beta-apo-13-carotenone.";
RL Biotechnol. Lett. 34:1851-1856(2012).
CC -!- FUNCTION: Catalyzes the conversion of 8'-apo-beta-carotenal to 13-apo-
CC beta-carotenone and C12-dialdehyde. Has also weak activity with 4'-apo-
CC beta-carotenal and gamma-carotene. {ECO:0000269|PubMed:22711425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-8'-apo-beta-carotenal + O2 = 13-apo-beta-carotenone
CC + 2,6-dimethyldeca-2,4,6,8-tetraenedial; Xref=Rhea:RHEA:36043,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:53154, ChEBI:CHEBI:53175,
CC ChEBI:CHEBI:73152; EC=1.13.11.82;
CC Evidence={ECO:0000269|PubMed:22711425};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22711425};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P74334};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for 8'-apo-beta-carotenal {ECO:0000269|PubMed:22711425};
CC KM=37 uM for 4'-apo-beta-carotenal {ECO:0000269|PubMed:22711425};
CC KM=203 uM for gamma-carotene {ECO:0000269|PubMed:22711425};
CC Note=kcat is 25 min(-1) with 8'-apo-beta-carotenal as substrate. kcat
CC is 8.4 min(-1) with 4'-apo-beta-carotenal as substrate. kcat is 0.2
CC min(-1) with gamma-carotene as substrate.
CC {ECO:0000269|PubMed:22711425};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:22711425};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:22711425};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22711425}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; CP000677; ABP64440.1; -; Genomic_DNA.
DR RefSeq; WP_011906827.1; NC_009427.1.
DR AlphaFoldDB; A4XES9; -.
DR SMR; A4XES9; -.
DR STRING; 279238.Saro_3580; -.
DR EnsemblBacteria; ABP64440; ABP64440; Saro_3580.
DR KEGG; nar:Saro_3580; -.
DR eggNOG; COG3670; Bacteria.
DR HOGENOM; CLU_016472_0_2_5; -.
DR OMA; WDINGEW; -.
DR OrthoDB; 389495at2; -.
DR BioCyc; MetaCyc:MON-17928; -.
DR Proteomes; UP000009134; Plasmid pNL2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..469
FT /note="8'-apo-carotenoid 13,14-cleaving dioxygenase"
FT /id="PRO_0000435392"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P74334,
FT ECO:0000305|PubMed:22711425"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P74334,
FT ECO:0000305|PubMed:22711425"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P74334,
FT ECO:0000305|PubMed:22711425"
FT BINDING 460
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P74334,
FT ECO:0000305|PubMed:22711425"
FT MUTAGEN 170
FT /note="H->A: Almost loss of activity. Strong decrease in
FT iron content."
FT /evidence="ECO:0000269|PubMed:22711425"
FT MUTAGEN 219
FT /note="H->A: Almost loss of activity. Strong decrease in
FT iron content."
FT /evidence="ECO:0000269|PubMed:22711425"
FT MUTAGEN 284
FT /note="H->A: Almost loss of activity. Strong decrease in
FT iron content."
FT /evidence="ECO:0000269|PubMed:22711425"
FT MUTAGEN 460
FT /note="H->A: Loss of activity. Strong decrease in iron
FT content."
FT /evidence="ECO:0000269|PubMed:22711425"
SQ SEQUENCE 469 AA; 51308 MW; FFA23CB5A20222FF CRC64;
MVTKGVVVVS SFRRSRQDAN RPHAFLTGIH APVKEERTIE DLAVTGTIPA ELSGRYVRIG
PNPFRADPRG HHWFVGDGMV HGVCMKGGKA LWYRNRYVRS RNLQDAGGPA AAPGPRRSTF
DTVNTNVIQH AGRTFALVEA GSFPVELTHD LESFAYSDLG GTLKGPFSAH PHLDPLTGEL
HAVTYDGQTL DTVWHVVVDR EGRVRREEPV PVAHGPSIHD CAITAKYVLI LDLPVTFSMA
ALVGGARFPY RWNPAHRARV GLLPREGTAA DVIWCDVDAA YVFHVANAFD NPDGTVTVDL
AAYETMFAHG PDGPNGKSLG MERWTVDPAA RKVARKTLDA APQEFHRPDE RFFGQPYRFA
WSMGLPAENA EDFLGHAPIY GYDLATGQRS AHDFGPGKIP GEFVFIPRRA DAEEGDGWLM
GYVIDLASET TDLAILDARN LAAPPLALIH IPCRIPPGFH GNWLPDAAD
