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Database: UniProt
Entry: A0A3N4RVA7_9ACTN
LinkDB: A0A3N4RVA7_9ACTN
Original site: A0A3N4RVA7_9ACTN 
ID   A0A3N4RVA7_9ACTN        Unreviewed;       962 AA.
AC   A0A3N4RVA7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:RPE36846.1};
GN   ORFNames=EDD38_5227 {ECO:0000313|EMBL:RPE36846.1};
OS   Kitasatospora cineracea.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE36846.1, ECO:0000313|Proteomes:UP000266906};
RN   [1] {ECO:0000313|EMBL:RPE36846.1, ECO:0000313|Proteomes:UP000266906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44781 {ECO:0000313|EMBL:RPE36846.1,
RC   ECO:0000313|Proteomes:UP000266906};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPE36846.1}.
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DR   EMBL; RKQG01000001; RPE36846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4RVA7; -.
DR   Proteomes; UP000266906; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          34..264
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          602..635
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   962 AA;  102823 MW;  EEFA48231A9B392B CRC64;
     MASDLARALA AAVRGEVRFD TAERAVYGQD ASNYRQVPRG VVKPVDGADV RAALRVCRER
     GVPVVARGSG TSIGGQAIGP GAVVLDFRRH FGRVLEVDPE RRTARVEPGA VLDELQRAAR
     PFGLRFGPDP STHSRCTIGG MVGNDACGSH SPAWGRTSDN LHGLDLLLSD GTELSVTGPL
     PPAERAALAA APGRIGRLHR ELQALAADNL ALLRRAMPVL PRRGSGYPLD ALLPERGYDL
     VRAVTGTEGT CALLLGATVR LVPEPAARAL VVAGYPDETA AADAVPALLP LAPLTCEGMA
     ADLVAALLAA GPRPPVLDRL PDGACWLFLE TGGATASEAA DRARELADAV RRERAAAVAL
     VTDPGEQRAL WAIREAGAGI VTRLPPGPDG RPGGAAWPGW EDSAVPVEQL GSYLRQLRTL
     LKRHGLRGVP YGHFGEGCVH LRLDFPLRER PEVFREFMTE AADLVVAHGG SLSGEHGDGQ
     ARAELLPRMF PPQVIDLFAR FKRIWDPEGL LNPGLLVDPR PLDADLRFPG RELPLALAYP
     EDGDSLLSAV HRCVGVGKCV DTSTGVMCPS YMVTGEERHS TRGRARLLGE MLRGELVTDG
     WRSPEVREAL DLCLGCKGCA SDCPVHVDMA SYRSEFLHHH YRFRPRPAAH LSFGWLPLWL
     RLAHLAPRAA NAVLRGRFSA PVLKRLGGID PRRELPALPE RRFSAWFRAH RAAHPADPGA
     PAVLLWPDSM SELLDPAPAR AAVLVLERLG FRVVLPPGPV CCGLTLIASG QLGLARRVVA
     RSVRNLGELP PGLPVVGLEP SCTATVRADW ARLLPGERPG LPSRIRTLAE FLDEREVELP
     ELTGPAMTQV HCHQHAVLGT GADRRITDRL GLTNRQLDAG CCGLAGAFGF ERGHWEVSVA
     AAERALLPAV RAAGPQTLLL ADGLSCRTQL TQLEPAARPL HLAEVLLRAF EQAGPGGGHS
     PG
//
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