ID   S7V6A7_9BACT            Unreviewed;       609 AA.
AC   S7V6A7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=FAD dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ADICYQ_5392 {ECO:0000313|EMBL:EPR65471.1};
OS   Cyclobacterium qasimii M12-11B.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR65471.1, ECO:0000313|Proteomes:UP000014974};
RN   [1] {ECO:0000313|EMBL:EPR65471.1, ECO:0000313|Proteomes:UP000014974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12-11B {ECO:0000313|EMBL:EPR65471.1,
RC   ECO:0000313|Proteomes:UP000014974};
RX   PubMed=23950138;
RA   Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT   from Arctic Marine Sediment.";
RL   Genome Announc. 1:e00642-13(2013).
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:EPR65471.1}.
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DR   EMBL; ATNM01000191; EPR65471.1; -; Genomic_DNA.
DR   RefSeq; WP_020889244.1; NZ_ATNM01000191.1.
DR   AlphaFoldDB; S7V6A7; -.
DR   STRING; 641524.ADICYQ_5392; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9780658at2; -.
DR   Proteomes; UP000014974; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR039650; HdrA-like.
DR   PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR   PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..609
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004545167"
FT   REGION          250..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  68650 MW;  E5043DD69165C1C2 CRC64;
     MKRILWIFAL LLGFTQMNPS QAQNRVLVEA ESFENTGGWV IDQQSFDVLY SSYLMAHGMG
     RVVEDASTKV NFQKGGTYHM WVRTKDWAPY PIGPGAFKLD INNKEIDQVF GQSGIVDWDW
     YYAGAVEMKQ GENSLTAKDL SGFNGRFDAI YFSTSKADKP TNDNKKLLTL RKELLGLTDG
     PEEIGKFDLV VVGGGIAGTT AAISAARMGL KVALIQNRPV LGGNNSSEIR VHLMGRVDVN
     HYPKLGRIVR ELDNGDPGNG NPDEKRYGDD RKLEIVRAEP NISLHLNTHV YEVEMDGNSI
     KAVIGRDIAT NQEYRFESTY FSDCTGDGTL GYLAGAEYRM GRESKEETGE SLAADTADDF
     TLGTSNLWAS LEKEYASDFP ETPWALQFSD EYHIDDHKAD WQWETGFGNF NTIYEAEQIR
     DHNLRAIFGN WSYLKKEKAE KYKNNELAWV SYIGGKRESR RLMGDHVLTQ MDIQDGVMYP
     DGSVTATWTI DLHFPDAKNS KYFEGEEFFA ATKHIRVKPY TIPYRALYSR NIDNLYMAGR
     NISTTHVAFG STRVMRTCGM MGEAVGYAAY VANRNGASPR EVYTRHLDEF MGIIESPLNI
     YNYPTLPNK
//