ID A0A1C6PM51_9ACTN Unreviewed; 1011 AA.
AC A0A1C6PM51;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:SCK44257.1};
GN ORFNames=H180DRAFT_03896 {ECO:0000313|EMBL:SCK44257.1};
OS Streptomyces sp. WMMB 322.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK44257.1, ECO:0000313|Proteomes:UP000182082};
RN [1] {ECO:0000313|EMBL:SCK44257.1, ECO:0000313|Proteomes:UP000182082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK44257.1,
RC ECO:0000313|Proteomes:UP000182082};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FMHI01000012; SCK44257.1; -; Genomic_DNA.
DR RefSeq; WP_055487362.1; NZ_FMHI01000012.1.
DR AlphaFoldDB; A0A1C6PM51; -.
DR STRING; 1286821.GCA_001418285_03879; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000182082; 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 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; 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; 2.
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; 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 50..279
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 988..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 108255 MW; 3EDC3B378C1C01CB CRC64;
MTAISGDAPS PAGTAETARH VEARLRGEIE GDVLFDEYTR HLFSRDASMY AIEPLGVVFP
RHAGDVQAAV TAAAEAGIPV VPRGAGTSLA GQTVGPGLVL DLSRHMNRIV EIDPEGRTAL
VEAGVVQDQL NRAAAAHGLM FGPDTSTSNR ATIGGMIGNN SAGSGSIRYG MTIDHVRELD
VVLSDSATAR LGPVDEAERG RRAGLPTLEG RLYRELPRIV EESAEATAEG MPQFWRRACG
YRLDRLAATG AEFDLAKFVV GSEGTLVLAT RALVDLVPKP SRTVIAVGHF TSVAGAIAAT
DDALACDPSA VEMMDRTILD LSRKKIEYAS LGSILEGDPE ALLFVSFTGD DEHELAGRLQ
QLTALWQRHG HGYHTLQAVT PAQQGSLLKV RKSSLGLLMA ASEGTRRPLA FIEDTAVDPV
HLGDYTRRFK QVLDRHGLNA GFYGHCSVGC LHIRPFVDTA DPVQVATMRS VAEEIKDLVR
EYGGVNSSEH GDGLARSEFN REIFGDDLYE AMRRVKGLFD PDNRLNPGKI VDAPSMTDNL
RDPALPPAGP LRTRLDFEVV GGMRGAADRC MNIGLCRKAG AGTMCPSYMA TLKEEDSTRG
RANALVKALS EPDPHRALGD GRLHEVLDLC LMCKACKSEC PLGVDMATLK AESLSHHHDE
HGIPRRSRVF ASIRRLNRIG SATAPLSNLP GRVPFLRALM DRYLGITPAR PLPAFVRGNL
VRWFRRRGRA AASPATATGP AAPGSQGTVT YLADSFTTYT EPGIGRAAVE LLELAGWHVT
LESRGCCGRS AFSKGLLDEA KDQARKLTKL LAQNSPAGSP VVGCEPSCLM TLRDEHRAML
PQDPAVADVS ARVRQAEELL AEAVDDGRLR LSPDAWPAGR RILYHGHCHQ KAEVGTAATV
ALLKRIPGAE VVELDAGCCG MAGSFGFESE HYETSMTVGS DRLFPAVRAE DDTTVIAASG
VSCRQQIFHG TERNAWHPVE LVRAALLTGS PDTGGTGDET PATATEGEAP R
//