ID   CRTNC_CYTFI             Reviewed;         453 AA.
AC   P0DPF0;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=4,4'-diapolycopene-4,4'-dial dehydrogenase {ECO:0000305};
DE            EC=1.2.99.10 {ECO:0000269|PubMed:25326460};
DE   AltName: Full=4,4'-diapolycopene aldehyde oxidase {ECO:0000303|PubMed:25326460};
DE   AltName: Full=4,4'-diapolycopene-4,4'-dial oxidase {ECO:0000305};
DE   AltName: Full=4,4'-diapolycopene-4,4'-dioate synthase {ECO:0000305};
GN   Name=crtNc {ECO:0000303|PubMed:25326460};
OS   Cytobacillus firmus (Bacillus firmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=1399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=GB1;
RX   PubMed=25326460; DOI=10.1099/mic.0.083519-0;
RA   Steiger S., Perez-Fons L., Cutting S.M., Fraser P.D., Sandmann G.;
RT   "Annotation and functional assignment of the genes for the C30 carotenoid
RT   pathways from the genomes of two bacteria: Bacillus indicus and Bacillus
RT   firmus.";
RL   Microbiology 161:194-202(2015).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=GB1;
RX   PubMed=22738026; DOI=10.1111/j.1365-2672.2012.05377.x;
RA   Steiger S., Perez-Fons L., Fraser P.D., Sandmann G.;
RT   "Biosynthesis of a novel C30 carotenoid in Bacillus firmus isolates.";
RL   J. Appl. Microbiol. 113:888-895(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the major C30 carotenoid
CC       4,4'-diapolycopene-4,4'-dioic acid, which protects B.firmus from
CC       peroxidative reactions (PubMed:22738026). Catalyzes the oxidation of
CC       4,4'-diapolycopene-4,4'-dial to yield 4,4'-diapolycopene-4,4'-dioic aci
CC       (PubMed:25326460). {ECO:0000269|PubMed:22738026,
CC       ECO:0000269|PubMed:25326460}.
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:0000269|PubMed:25326460};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305|PubMed:22738026}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DPF0; -.
DR   SMR; P0DPF0; -.
DR   BRENDA; 1.2.99.10; 653.
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; IPR016160; Ald_DH_CS_CYS.
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   PANTHER; PTHR43570; PTHR43570; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Oxidoreductase.
FT   CHAIN           1..453
FT                   /note="4,4'-diapolycopene-4,4'-dial dehydrogenase"
FT                   /id="PRO_0000443511"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   453 AA;  50131 MW;  3BD637ED10855269 CRC64;
     MPDNDSHSLK SLPERQREDL FSAGSPSLEA RKKQLSRLKT MIVDHEEAFT RALHADLGKP
     AFESFSSEIA VLLNEIDHVC KHIAKWNRQS RSRYLKMGYV ESIKRKRHPY GSVLIIGSWN
     YPLQLSLMPA IGAIAAGNRC VIKPSEHAPA TAELLKKIIN DAFPPEQLLV VTGDAQTASH
     LTAAPFDLIF FTGSGQTGKA VAEQAARQLT PVILELGGKN PCIIDETGFS KEAVREIVWG
     KFLNAGQTCI APDTLFVHQS VYEKMLNEIS AAVSAFYGEQ PRESSDYGRI CTDDHFQKVI
     EFIGQGDVRH GGSYDRSDRF IAPTVLTDIE PGSPILQEEI FGPVLPVIPY TDMRTLLSSG
     RIQRDALTGY IFSKNKDNIQ LFKEHMRSST ISVNQVIHHA ASPHIAFGGV GTSGYGAYHG
     KAGFLAFSYE KQNTEHIITS IFKVNSRHIL IQI