ID   ALD_METSP               Reviewed;         530 AA.
AC   Q4VKV0;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=4,4'-diapolycopene aldehyde oxidase {ECO:0000303|PubMed:15933032};
DE            EC=1.2.99.10 {ECO:0000305|PubMed:15933032};
DE   AltName: Full=4,4'-diapolycopenedial dehydrogenase {ECO:0000305};
DE   AltName: Full=4,4'-diapolycopenoate synthase {ECO:0000305};
GN   Name=ald {ECO:0000303|PubMed:15933032}; Synonyms=crtNc {ECO:0000305};
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, AND PATHWAY.
RC   STRAIN=16a {ECO:0000312|EMBL:AAX46184.1};
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 4,4'-diapolycopene-4,4'-dial to yield 4,4'-
CC       diapolycopene-4,4'-dioic acid. Also able to catalyze the oxidation of
CC       4,4'-diapolycopen-4-al to yield 4,4'-diapolycopen-4-oic acid.
CC       {ECO:0000269|PubMed:15933032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + all-trans-4,4'-diapolycopen-4-al + H2O = AH2 + all-trans-
CC         4,4'-diapolycopen-4-oate + H(+); Xref=Rhea:RHEA:44716,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:138599, ChEBI:CHEBI:138600;
CC         EC=1.2.99.10; Evidence={ECO:0000305|PubMed:15933032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 A + all-trans-4,4'-diapolycopene-4,4'-dial + 2 H2O = 2 AH2 +
CC         all-trans-4,4'-diapolycopene-4,4'-dioate + 2 H(+);
CC         Xref=Rhea:RHEA:42380, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:62450,
CC         ChEBI:CHEBI:79063; EC=1.2.99.10;
CC         Evidence={ECO:0000305|PubMed:15933032};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305|PubMed:15933032}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce 4,4'-
CC       diapolycopene dialdehyde in addition to the 4,4'-diapophytoene
CC       precursor. {ECO:0000269|PubMed:15933032}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AY841893; AAX46184.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4VKV0; -.
DR   SMR; Q4VKV0; -.
DR   KEGG; ag:AAX46184; -.
DR   BioCyc; MetaCyc:MON-16326; -.
DR   BRENDA; 1.2.99.10; 3315.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Oxidoreductase.
FT   CHAIN           1..530
FT                   /note="4,4'-diapolycopene aldehyde oxidase"
FT                   /id="PRO_0000443512"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   530 AA;  58539 MW;  B560E1B089EDA699 CRC64;
     MTTIAAVSPL DGRLLGHFPV SKPALIQQQL TKSRRAALLW RELPVTERVK RLSPLKKQLL
     DNLDRLCETI RLSTGKVRTE ALLGEIYPVL DLLAYYQKRA PRILRTRAVS TSPFAFPAAT
     ARIERRPYGV VAVISPWNYP FHLSVAPLLT ALLAGNAVIL KPSELCLPVG QLIVDLFATL
     DLPDGLVQWV IGDGQTGAEL IDARPDLVFF TGGLQTGRAV MQRAARHPIP VMLELGGKDT
     MLVLADADLK RASAAALYGA FCNSGQVCVS VERLYVQQAC FAEFLAMLLK GLSKLKVGHD
     PHGDVGVMTS ARQIDIVQAH YEDAIAQGAK ASGPLLRDGN VVQPVVLWDV HHGMKVMREE
     TFGPLLPVMP FSDEAEAIKL ANDSDLGLNA SIWSQDIIKA ERLAGQLDVG NWAINDVLKN
     VGHSGLPFGG VKQSGFGRYH GAEGLLNFSY PVSGLTNRSR LPKEPNWFPY SASGYENFKG
     FLDFIYGEDS MLQRGRRNQQ ALQAFREFSI FDWTQRWQNL KLLFSWTRDD