ID   M0CHS2_9EURY            Unreviewed;       534 AA.
AC   M0CHS2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Lycopene beta and epsilon cyclase {ECO:0000313|EMBL:ELZ22173.1};
GN   ORFNames=C476_07082 {ECO:0000313|EMBL:ELZ22173.1};
OS   Natrinema limicola JCM 13563.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ22173.1, ECO:0000313|Proteomes:UP000011615};
RN   [1] {ECO:0000313|EMBL:ELZ22173.1, ECO:0000313|Proteomes:UP000011615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ22173.1,
RC   ECO:0000313|Proteomes:UP000011615};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:ELZ22173.1}.
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DR   EMBL; AOIT01000029; ELZ22173.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0CHS2; -.
DR   STRING; 1230457.C476_07082; -.
DR   PATRIC; fig|1230457.4.peg.1419; -.
DR   eggNOG; arCOG02233; Archaea.
DR   Proteomes; UP000011615; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011615}.
FT   DOMAIN          200..230
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   534 AA;  57864 MW;  20D745C1B8672AC5 CRC64;
     MPATDTDADR TPVGDADVCV IGAGPAGGLV ADRLAEAGHE VVILEAGPRF DSADRLARQE
     RGIRPAYDRP AIWDSDPERD AYESSGERFY PLNHARARGV GGSTLHWQGM VMRLHEADFN
     SASIRGVGTD WPIDYEDLRP YYAAAERELG VAGADDNPFA PPREEPHPMP AFRPSYSDSL
     FAEACDGLEI AMHSVPNARN SEAYDGRNAC VGYGTCQPVC PSGAKYDATV HVKRAERKGA
     TVIDRAPVQR LEHGPDTIEA AVYATPDGEA HRQEADAFVI ACGGVETPRL LLLSESSHYP
     DGLANSSGLV GTFFMDHLFA GTGGVLDEPT RQNHVGFLTS ESHQFYDEAD AEYAPFKLEF
     FNYAGPSPVG MALTGDDWGD DLLARLRSEY GSHVGMGGLV EQLPRENSYV GLDASTTDDH
     GNPVPDVHWN VGERALRTIE RVNEIQERIL DELGAEITWQ VGRENTGPAY HHMGTTRMGD
     DPTESVVGPD LRTHDLENCW IASSSVFPTG GAMNPTLTIA ALALKAADHI LERL
//