ID   CARD_GIBF5              Reviewed;         539 AA.
AC   F6IBC7; S0E1W7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 2.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Beta-apo-4'-carotenal oxygenase;
DE            EC=1.2.1.82;
DE   AltName: Full=Beta-apo-4'-carotenal dehydrogenase;
GN   Name=carD; ORFNames=FFUJ_07503;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP   INDUCTION.
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=21749649; DOI=10.1111/j.1742-4658.2011.08242.x;
RA   Diaz-Sanchez V., Estrada A.F., Trautmann D., Al-Babili S., Avalos J.;
RT   "The gene carD encodes the aldehyde dehydrogenase responsible for
RT   neurosporaxanthin biosynthesis in Fusarium fujikuroi.";
RL   FEBS J. 278:3164-3176(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- FUNCTION: Beta-apo-4'-carotenal oxygenase involved in the last step od
CC       synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an
CC       essential protective pigments and leading to orange pigmentation. Is
CC       also able to use shorter apocarotenals as substrates (such as beta-apo-
CC       8'-carotenal (C30), beta-apo-10'-carotenal (C27), or the acyclic
CC       apocarotenal apo-8'-lycopenal (C30)), indicating wide substrate
CC       specificity. {ECO:0000269|PubMed:21749649}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-apo-beta-carotenal + H2O + NAD(+) = 2 H(+) + NADH +
CC         neurosporaxanthin; Xref=Rhea:RHEA:31515, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:53157, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:63069; EC=1.2.1.82;
CC         Evidence={ECO:0000269|PubMed:21749649};
CC   -!- INDUCTION: Expression is increased about three-fold after 30 min of
CC       illumination, and decreased thereafter. {ECO:0000269|PubMed:21749649}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCA63431.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; FR850689; CCA63431.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; HF679027; CCT68695.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6IBC7; -.
DR   SMR; F6IBC7; -.
DR   STRING; 1279085.F6IBC7; -.
DR   EnsemblFungi; CCT68695; CCT68695; FFUJ_07503.
DR   KEGG; ag:CCA63431; -.
DR   VEuPathDB; FungiDB:FFUJ_07503; -.
DR   HOGENOM; CLU_005391_3_1_1; -.
DR   BRENDA; 1.2.1.82; 2425.
DR   Proteomes; UP000016800; Chromosome 5.
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   PANTHER; PTHR43570; PTHR43570; 1.
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; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..539
FT                   /note="Beta-apo-4'-carotenal oxygenase"
FT                   /id="PRO_0000418443"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         206..211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        273
FT                   /note="S -> G (in Ref. 1; CCA63431)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   539 AA;  59891 MW;  1BF6A96A56C6CDC5 CRC64;
     MAANNLSYTI APLEHTPLDE IAAKVDLVRK TFRSGRTKDM EFRMKQIRKL YWAIVDNTEL
     MQDALIKDLR KCKYEAVLAE IDWCKQECID MVNNMEKWLR DEPVPNVPLQ FRAMKHRTRF
     EPLGVVLNIG SFNFPFQLNL PVVIGAIACG NCVVLKASES SPNCAMVLKK IFDESLDPEC
     FTYVNGALPE TQLLLEQKFD KICFTGGKAV GKIIAQKAAE TLTPVLLELG GLNPAFVTKH
     ANLKLAARRL LWQKSLNAGQ VCMSHNYILV ERSVLSQFLG ELNNQMRTFF PQGAKNSPDL
     CRIVNAGHFN RLKKMLDGTN GKIVLGGSMD ESTLFMEPTA VLVDDINDSM MTQEAFGPIF
     AMMAVDSLDQ AIDIANTVDP TPLSLSAFGS KAENNKILDN VTSGGATCND AFFHSQIPQS
     PLGGVGQSGM GNYHGIYSIR TFSHQRTIAE VPYWADFLFR VRYMPYQWPV MNRMKAVADS
     KPNFDRNGNK TKGITYFLAL VLGLGSKKSK GALLRWAVLV VAAAILEAKK GVLSQLLTR