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Database: UniProt
Entry: A0A068SB36_9FUNG
LinkDB: A0A068SB36_9FUNG
Original site: A0A068SB36_9FUNG 
ID   A0A068SB36_9FUNG        Unreviewed;       690 AA.
AC   A0A068SB36;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   SubName: Full=Betacarotene-monooxygenase {ECO:0000313|EMBL:CDH59175.1};
GN   ORFNames=LCOR_10002.1 {ECO:0000313|EMBL:CDH59175.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH59175.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH59175.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDH59175.1}.
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DR   EMBL; CBTN010000066; CDH59175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068SB36; -.
DR   STRING; 1263082.A0A068SB36; -.
DR   VEuPathDB; FungiDB:LCOR_10002.1; -.
DR   OrthoDB; 294919at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; 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; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Monooxygenase {ECO:0000313|EMBL:CDH59175.1};
KW   Oxidoreductase {ECO:0000313|EMBL:CDH59175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         368
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         436
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   690 AA;  76216 MW;  AE179E403E2D8062 CRC64;
     MSDKADVEHP LTPTREDQAT SDESFSVISE SAVADKPADS DESEWKNVSS DNSDDDQAKR
     ATSHPLQQSS AIDVSAYSND TWSQQQESSL LDAEGLPNAQ DGDSGATTPV KEREIELDSD
     TSHIKGFANA GDIDGIADLE VEGQLPEWLN GEHYTIGPGT YDIRYTRKIE IDGLLQSATA
     TFSFGHWFDG LPLANRFDFN GKRNAITYRS RLTCRRLVEK IRDHHGYAPP HPAGLFKTDS
     NQTMLVKFLK SAPKANKPDA EPCAARILAG IPGVDGRLFA QNYANHIQEL DPFDLKPTRV
     LCWNEVNPAF KGYSSCPNGQ YDPQTGEYIN FTMEIGYQST AYNFFSISDR NPKGSIIASV
     TAPTGYVHSF SLTPKYIVLV VFPLLTNTGA VKFAWNESIM DSFSFYPSEP TLFYVISRDK
     GQHLVTYRAD ACFAFHHVNA YEDGHDNINV DILCYKDATI AHQLTTENMR NPSEMKPSRL
     APSELRRFVL SNIEDESLSY LTNNSILPTA SGVASRVSSM WSYLRGTNAT TDVENSTAQP
     SAAAAGWYAT LPVASSGQLV QSSMELPQVN PLYRMHRHKY VYGVGFSEES DGKIWDSIIK
     TDIETHKVTA AWHQENCYPS EAVFIGRPSA SADEELQEDD GVLVSIVLDS ARATSFLLVL
     DASNLQVLAK AYLGVLVPLS FGRGSYRLRT
//
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