ID   Y1602_METBF             Reviewed;         387 AA.
AC   P96800; Q46C44;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Uncharacterized protein Mbar_A1602;
DE   AltName: Full=ORF3;
GN   OrderedLocusNames=Mbar_A1602;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
RX   PubMed=9063468; DOI=10.1111/j.1432-1033.1997.00226.x;
RA   Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.;
RT   "Heterodisulfide reductase from methanol-grown cells of Methanosarcina
RT   barkeri is not a flavoenzyme.";
RL   Eur. J. Biochem. 244:226-234(1997).
CC   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. ChlP
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA70994.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000099; AAZ70548.1; -; Genomic_DNA.
DR   EMBL; Y09870; CAA70994.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P96800; -.
DR   SMR; P96800; -.
DR   STRING; 269797.Mbar_A1602; -.
DR   EnsemblBacteria; AAZ70548; AAZ70548; Mbar_A1602.
DR   KEGG; mba:Mbar_A1602; -.
DR   eggNOG; arCOG00570; Archaea.
DR   HOGENOM; CLU_024648_5_0_2; -.
DR   OMA; HAIAYMT; -.
DR   OrthoDB; 31233at2157; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..387
FT                   /note="Uncharacterized protein Mbar_A1602"
FT                   /id="PRO_0000219668"
FT   CONFLICT        236
FT                   /note="V -> I (in Ref. 2; CAA70994)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  43769 MW;  EFBB5E845F9AB1B1 CRC64;
     MISMKKYDVV IIGAGPAGSY AAYMLAKSKI NVLVIDKYSF PRYKPCAGGL TAKAFNSFDF
     PISKEVKYST NSIVTSYKNQ IFHNISGNKT LVKMIERKEF DDFLIKKAVD SGATFLDGMK
     VTEITWENAE FSIKTDSEFF RCNYLIGADG TNGIVNRTFN IVERDLYGFA VEINCPVSRD
     NIGKFNMTFD FGTVPNGYLW IFPKDEYVCV GAYTTNRKMK NIQKYLLDYI EKLGLVPESE
     KLKGHIIPYY GINYKQPDFP CVLVGDAAGF GEYWTGEGIY YAVKSGTIAA EVISSSIKSG
     IFDRQALQRR YQREIIRGLK LAYYIGKFFY GNLPLSFNLV MSYLPVGIMY ESASRGLTFD
     QSFSKIHVAL SSLILNKSHI SNNKYHR