ID   M0K2Y4_9EURY            Unreviewed;      1012 AA.
AC   M0K2Y4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:QUJ72359.1};
DE   SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:EMA15526.1};
GN   ORFNames=C436_03296 {ECO:0000313|EMBL:EMA15526.1}, KDQ40_00985
GN   {ECO:0000313|EMBL:QUJ72359.1};
OS   Haloarcula sinaiiensis ATCC 33800.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA15526.1, ECO:0000313|Proteomes:UP000011659};
RN   [1] {ECO:0000313|EMBL:EMA15526.1, ECO:0000313|Proteomes:UP000011659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA15526.1,
RC   ECO:0000313|Proteomes:UP000011659};
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).
RN   [2] {ECO:0000313|EMBL:QUJ72359.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ72359.1};
RA   Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT   "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT   Haloarcula sinaiiensis.";
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AOLR01000005; EMA15526.1; -; Genomic_DNA.
DR   EMBL; CP073366; QUJ72359.1; -; Genomic_DNA.
DR   RefSeq; WP_004958213.1; NZ_CP073366.1.
DR   AlphaFoldDB; M0K2Y4; -.
DR   GeneID; 64821487; -.
DR   KEGG; hsin:KDQ40_00985; -.
DR   PATRIC; fig|662476.7.peg.655; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000011659; Unassembled WGS sequence.
DR   Proteomes; UP000682967; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          57..293
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          649..681
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          971..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  110604 MW;  E85404D9863E75BC CRC64;
     MAIENIEDTW SAQELDLNRP DVDAYRDLAE ALRARVTGGV EFDEYARILY ATDGSIYRAE
     PAGVVYPTDI DDVRAAVEVA TSHGVPILPR GTGSSLAGQT VGPGCVVLDM SRHMDDILDI
     RPDEQTAHIQ PGVVQDDLDD TLANYGLKFA PDPASSNRAS VGGGIGNNST GAHSVRYGIT
     DAYTDAVKAV LSDGSLIHAR EVVIDSPEWD DIVSKDDREA DIYQTVREVV EENANEIEDR
     YPDLKRRVSG YNLDRVTYEN DDGERVLNLA KLFVGSEGTL GVIVEAELSL VTVPEETALA
     LYCFDTLPDA MRAVPVALDY DVSAVELMDD EMFRLAAGSD GYAEYVDPIP DRAAAALMLE
     YDSELHDDFE AAIARTNERF LDNGAAFDVV EAYTDADQAD LWKLRKAAIP LLMSMDGDPK
     PYPFIEDATV PPAELAEYVE KFEEVLADHD TSAAYFAHAG SGTLHIRPIL NLKEESGIED
     MHSITDDVTD LVLEHNGSFS GEHGDGMART EFTPKMYGET LWDAFKQVKT AFDPQWWMHP
     GNVVYRDGPA DIGPDADRGV GADMRENLRY GPDYQSLEPQ TTLDFEDEGG FSELVELCNG
     CGTCRQTDGD VMCPTYRASE EEVQTTRGRA NLLRSAISGD LDEDEIHSDR FQEEVLDLCV
     GCKGCKSDCP TGVDMAKLKT ELKHQHHEAE GASLRERLFA NIDTASKLGS ALAPISNWAT
     DIPGARAVMQ KLFGIAPERE LPTFSRETLQ DWFDARGGST VSRAEADRKV LLFPDTYTNY
     SYPTAGKAAV ETLEAAGVHV TIPDNTAPSG RAAYSTGMLD VARDRAETNT DRLADRVTEG
     WDIVFVEPSD AVMFQDEYLD LLDGSAVSQV ADSAYGVLEY LDTFRLDDAL PVEDRSLGAA
     GAVSYHGHCN QKGTNKDHHA VGVMRRVGYE VDPLDSTCCG MAGSFGYHDE HYDLSKTIGR
     LLFDKVEESD GDRVVAPGGS CRSQLGDRDG VDEIPPHPIE VVAERVPETT TS
//