ID A0A291QNJ7_9ACTN Unreviewed; 1135 AA.
AC A0A291QNJ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:ATL33114.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:ATL33114.1};
GN ORFNames=KY5_8096 {ECO:0000313|EMBL:ATL33114.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL33114.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL33114.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL33114.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP022685; ATL33114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291QNJ7; -.
DR KEGG; sfk:KY5_8096; -.
DR Proteomes; UP000221011; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ATL33114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221011}.
FT DOMAIN 2..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 791..902
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1053..1135
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 123415 MW; 15C863191AD6825C CRC64;
MIEERRSFCT LCKSRCGAIY TVTDGRITDV RPDPEHPTGA AMCPKGKSAP EIAHSTRRLT
TPLRRTNPKS HPDPGWRPIS WDEALDEIAE RMREIAAESG PEAVAFAVAT PSGTMVSDAT
EWIERFIRLF GSPNTVYSAE ICNWHKDFAH AFTFGTPLPP PDYAHADLAL LWGFNPAKTW
LSQSAAVSAA QARGMRLAVV DPRRSTSALR ADHWLRVRPG TDAALALGLA HLLIENGSYD
EEFVRTWTNG PLLVRRDNGR FLRADELAAE TQGFVVWDEA DDGPRAYDTH AAARSPERFA
LRGAHRVRTL RGSVLCEPAF ERYARACAEW PAERVAHTTW IPEPEIRALA EEIGAARSVT
YYGWTGVGQS ANAAQTERAL ATLYALTGSY DTEGGNHLVP PPPYNPATWA GQLAPEQRAK
ALGIDKHPLG PPASGYVNAG DLCRAIETQE PYAVRALIGF GSNLVVAQPD SDRVARALRS
LEFQVHLDLF ANPTSTTADI VLPVNSAYEH EALRFGFEID HRAQEHTQLR PRLTEPVGTS
RSDTEVVFDL ACRLGMGEEF FGGDVEAAWN WQLEPLGLTV GELRGRPGGV RVPRPRALRK
YARRTGEPAA PGGEAVAGFG TPTRRVELYS ERLWEHGHPA VPEHRSPVEP DAAFPLVLTC
AKHGHFVHSQ HRSLTTLRRR SPDPCVDMSP EAAAARGISE GQWVELSTRL GGIRLRARFD
GSLHPSVVVS EYGWWQDAPD LALPGADPVS GEGSNLNRLI GYEGSDPLSG SVPLRASVCE
IRPLPSDGTW SGTRPFTVTA VGAEGSGVRT LRLEPADGGP LPDYRPGQHV TVHAEDASGA
ARHPSLGRSY SLTGPATAPA RTSYDLAVRH VPDGSFSTYV HEELRAGSRL HLSAPGGTFR
IPSDTATPVV LLAGGIGVTP FMSYLETLAA SGGTVPEVVL HHGNTNSADH PFRTRLHELR
GRVRALRIID HYTAPGADDV LGRDHERRGF ITADDIDPEL IARRARFYLC GPLPMLDALT
EGLRARGVPR FEIFSERFRS APREVDVPDD AEFAVRFARS GRSVTWRTTD GSLLELGERA
GVSLPSGCRV GQCESCACTV LTGRATSLVR VPDDLPEETV LTCQSVPASD LVLDA
//
