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Database: UniProt
Entry: M1Y546_NATM8
LinkDB: M1Y546_NATM8
Original site: M1Y546_NATM8 
ID   M1Y546_NATM8            Unreviewed;       532 AA.
AC   M1Y546;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:CCQ37672.1};
GN   OrderedLocusNames=Nmlp_3548 {ECO:0000313|EMBL:CCQ37672.1};
OS   Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS   8.8.11).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37672.1, ECO:0000313|Proteomes:UP000011867};
RN   [1] {ECO:0000313|EMBL:CCQ37672.1, ECO:0000313|Proteomes:UP000011867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC   {ECO:0000313|Proteomes:UP000011867};
RX   PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA   Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA   Gross K., Schuster S.C., Oesterhelt D.;
RT   "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT   of a previously haloalkaliphilic genus.";
RL   Genome Announc. 1:e0009513-e0009513(2013).
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}.
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DR   EMBL; HF582854; CCQ37672.1; -; Genomic_DNA.
DR   RefSeq; WP_015410409.1; NC_020388.1.
DR   AlphaFoldDB; M1Y546; -.
DR   STRING; 268739.Nmlp_3548; -.
DR   GeneID; 14652599; -.
DR   KEGG; nmo:Nmlp_3548; -.
DR   eggNOG; arCOG02233; Archaea.
DR   HOGENOM; CLU_008878_4_1_2; -.
DR   OrthoDB; 346033at2157; -.
DR   Proteomes; UP000011867; Chromosome.
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:UP000011867}.
FT   DOMAIN          198..228
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   532 AA;  57301 MW;  B488AB6344886796 CRC64;
     MNGGGATDRS PVPDADVCIV GAGPAGALVA DRLAADHEVV VLDAGPRFDP ADRLERQERA
     IRPAYDRPDV WDGDPERDAH SASGEWFYPL NHARIKGIGG STLHWQGMVM RLHEDDFDSG
     TERGVGPDWP IDYADLRPHY AAAERELGVA GADDNPDAPP REEPFPMPAF PPSYSDGLFA
     EACEALGIDM HSVPNARNSE TYDGRSACVG YGTCQPVCPS GAKYDATVHV ERAESKGATV
     IDRAPVQRLE HDADRVRAAV YATPDGTEHR QAADAVVVAC GGVETPRLLL LSESEQYPDG
     LANSSGLVGR YFMDHLFAGT GGVLEEPTRQ NHVGFLTSES HAFYDDADED IAPFKLEFFN
     YDGPSPAEAA LSADTWGDEL LEQLREDYGT HIGMGALVEQ LPREDSYVGL DPDRTDDHGN
     PVPDVHWNVG DRALRSIERA NEIQASILSE LGAEITWQVG PDDTGPAYHH MGTTRMGTDP
     DASVVDPHLR THDLGNCWLV TSGAFPTGGA VNPTLTIAAL ALRAAEDVRD AL
//
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