CRTP_METSP
ID CRTP_METSP Reviewed; 497 AA.
AC Q4VKU9;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=4,4'-diapolycopene oxygenase {ECO:0000305};
DE EC=1.14.99.44 {ECO:0000269|PubMed:15933032};
DE AltName: Full=4,4'-diapolycopene oxidase {ECO:0000303|PubMed:15933032};
DE AltName: Full=4,4'-diaponeurosporene oxidase {ECO:0000303|PubMed:15933032};
DE AltName: Full=Carotenoid oxidase {ECO:0000303|PubMed:15933032};
DE AltName: Full=Diaponeurosporene oxygenase {ECO:0000303|PubMed:15933032};
DE EC=1.14.99.- {ECO:0000305|PubMed:15933032};
GN Name=crtNb {ECO:0000303|PubMed:15933032};
OS Methylomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=418;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, PATHWAY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=16a {ECO:0000312|EMBL:AAX46185.1};
RX PubMed=15933032; DOI=10.1128/aem.71.6.3294-3301.2005;
RA Tao L., Schenzle A., Odom J.M., Cheng Q.;
RT "Novel carotenoid oxidase involved in biosynthesis of 4,4'-diapolycopene
RT dialdehyde.";
RL Appl. Environ. Microbiol. 71:3294-3301(2005).
CC -!- FUNCTION: Involved in the biosynthesis of C30 carotenoids. Catalyzes
CC the oxidation of the terminal methyl side groups of 4,4'-diapolycopene
CC to yield 4,4'-diapolycopen-4,4'-dial via the aldehyde intermediate
CC 4,4'-diapolycopen-al. Also able to catalyze the oxidation of the
CC terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'-
CC diaponeurosporen-4-al. It has moderate to low activity on the C40
CC substrates neurosporene and lycopene, and has no detectable activity on
CC zeta-carotene or beta-carotene. {ECO:0000269|PubMed:15933032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 AH2 + all-trans-4,4'-diapolycopene + 4 O2 = 4 A + all-trans-
CC 4,4'-diapolycopene-4,4'-dial + 6 H2O; Xref=Rhea:RHEA:31019,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:62449, ChEBI:CHEBI:62450;
CC EC=1.14.99.44; Evidence={ECO:0000269|PubMed:15933032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 AH2 + all-trans-4,4'-diaponeurosporene + 2 O2 = 4,4'-
CC diaponeurosporenal + 2 A + 3 H2O; Xref=Rhea:RHEA:56104,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:62743, ChEBI:CHEBI:79065;
CC Evidence={ECO:0000305|PubMed:15933032};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P21685};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305|PubMed:15933032}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate the fully
CC unsaturated C30 carotenoid backbone 4,4'-diapolycopene with some
CC additional less unsaturated intermediates.
CC {ECO:0000269|PubMed:15933032}.
CC -!- MISCELLANEOUS: CrtNb is not a carotenoid desaturase, in spite of its
CC apparent sequence homology. {ECO:0000305|PubMed:15933032}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AY841893; AAX46185.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4VKU9; -.
DR SMR; Q4VKU9; -.
DR BioCyc; MetaCyc:MON-16324; -.
DR BRENDA; 1.14.99.44; 3315.
DR BRENDA; 1.2.99.10; 15636.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..497
FT /note="4,4'-diapolycopene oxygenase"
FT /id="PRO_0000443513"
SQ SEQUENCE 497 AA; 55574 MW; 4C03FFDCCE4FF348 CRC64;
MNSNDNQRVI VIGAGLGGLS AAISLATAGF SVQLIEKNDK VGGKLNIMTK DGFTFDLGPS
ILTMPHIFEA LFTGAGKNMA DYVQIQKVEP HWRNFFEDGS VIDLCEDAET QRRELDKLGP
GTYAQFQRFL DYSKNLCTET EAGYFAKGLD GFWDLLKFYG PLRSLLSFDV FRSMDQGVRR
FISDPKLVEI LNYFIKYVGS SPYDAPALMN LLPYIQYHYG LWYVKGGMYG MAQAMEKLAV
ELGVEIRLDA EVSEIQKQDG RACAVKLANG DVLPADIVVS NMEVIPAMEK LLRSPASELK
KMQRFEPSCS GLVLHLGVDR LYPQLAHHNF FYSDHPREHF DAVFKSHRLS DDPTIYLVAP
CKTDPAQAPA GCEIIKILPH IPHLDPDKLL TAEDYSALRE RVLVKLERMG LTDLRQHIVT
EEYWTPLDIQ AKYYSNQGSI YGVVADRFKN LGFKAPQRSS ELSNLYFVGG SVNPGGGMPM
VTLSGQLVRD KIVADLQ
