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Database: UniProt
Entry: A0A256H7H0_9EURY
LinkDB: A0A256H7H0_9EURY
Original site: A0A256H7H0_9EURY 
ID   A0A256H7H0_9EURY        Unreviewed;       987 AA.
AC   A0A256H7H0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:OYR40046.1};
GN   ORFNames=DJ82_08395 {ECO:0000313|EMBL:OYR40046.1};
OS   Halorubrum sp. Ib24.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1383850 {ECO:0000313|EMBL:OYR40046.1, ECO:0000313|Proteomes:UP000216554};
RN   [1] {ECO:0000313|EMBL:OYR40046.1, ECO:0000313|Proteomes:UP000216554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ib24 {ECO:0000313|EMBL:OYR40046.1,
RC   ECO:0000313|Proteomes:UP000216554};
RX   PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA   Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA   Ventosa A., Gogarten J.P., Papke R.T.;
RT   "Population and genomic analysis of the genus Halorubrum.";
RL   Front. Microbiol. 5:140-140(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OYR40046.1}.
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DR   EMBL; NHOX01000032; OYR40046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256H7H0; -.
DR   Proteomes; UP000216554; Unassembled WGS sequence.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000216554}.
FT   DOMAIN          59..291
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          635..667
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  107313 MW;  34ADAD204EA5A351 CRC64;
     MGSKNTTPDP STDPRANYDY QSETEHDSSL VADLDALVDG DVRFDEYSKQ MYATDASAYE
     VTPIGVVYPT STADVAAVME YCAAEEIPAL PRGGGTSLAG QSVNEAIVLD FTRYMTDVVD
     VDPEGERARA RTGITLGELN RTLEPHGLKF APDPSTADRS ALGGAIGNNT TGAHSLKYGK
     TDAYVEEVEA VLADGSVETF GEVSVAELRG AADPDGTTLE RIYAEIVRII DEEADEVDER
     YPDLKRNVSG YNLDVLIEEA ESGTVNLARL LVGSEGTLAI VTEAEVSLEP IPETKGVALL
     TYHDLLDAME DVGPILEHDA AAVEVLDGVL VDLARELEEF KDVIGLLPDE TDSFLLIEFY
     ADDEESAKRQ VDDLIEDRVG DLAFDGMAAY DEETQKKFWK MRKASTPILL SRTGDEKHIA
     FIEDLAIPPE HLPEYTKEFK EIFEDHDTFG SFYAHAGPGC MHVRPLINTK NAEGTETMVS
     ISDAATDLAV KYGGSVSGEH GDGRARTQWN RKLYGDRLWH VFQDLKTAFD PDWLLNPGSV
     CGDHDMSENL RFGEEYEFDA GFEPALEWEN ENGFQGMAEL CHGCGGCRTS QEGAGGVMCP
     TYRASQEEIT STRGRANLLR QAMSGDLSED EQFDTEFMRE VLDLCVGCKG CSIDCPSEVD
     MAKMKVEVEH AHHEEHGADL RSKLFANVDA LSKLGSATAP LSNLGTKVPG ARVVMEKTLG
     IARERSLPTF HRETFVDWWA DRGGSTVSES TADRRVVLVP DTVTNYNNPK AGKAAVRVLE
     AAGVHVSVAE EITDSGRPAH SKGLLGKARE TAEANVATLA AHVDDGRDVV VVEPSDAVML
     QSDYLDLLSS DAAAQVAEHA YGVLEYLDTR RLDEALDADG GAERLTYHGH CHQKSVKKDH
     HAVGVLRRTG FRVDPLDTSC CGMAGTFGYE SEHYSMSQAI GSMLFDRIDD SDGDSVVAPG
     ASCRTQIGDE YDEKPPHPIE KIADALA
//
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