ID A0A554V7C0_9ACTN Unreviewed; 727 AA.
AC A0A554V7C0;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Molybdopterin-dependent oxidoreductase {ECO:0000313|EMBL:TSE01182.1};
GN ORFNames=FOS14_05430 {ECO:0000313|EMBL:TSE01182.1};
OS Skermania sp. ID1734.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Skermania.
OX NCBI_TaxID=2597516 {ECO:0000313|EMBL:TSE01182.1, ECO:0000313|Proteomes:UP000320451};
RN [1] {ECO:0000313|EMBL:TSE01182.1, ECO:0000313|Proteomes:UP000320451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ID1734 {ECO:0000313|EMBL:TSE01182.1,
RC ECO:0000313|Proteomes:UP000320451};
RA Kim D.-U.;
RT "Skermania sp. nov. isolated from car air conditioner.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:TSE01182.1}.
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DR EMBL; VLIY01000003; TSE01182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A554V7C0; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000320451; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000320451}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 727 AA; 79856 MW; 0B7CB3BDD3F68B01 CRC64;
MQQEKVTFCR ICEPFCGMIA TVENDRLIGL RPDKDHPLSR GFACPKGMAY PAVQNDPDRV
LHPLRKRPDG TFEQVSWHEA TSEIARRVRH IRSRYGARSG AFYLGNPAAL NYSNALWSLL
FMRALGITHF FSAGSQDTNS RFVANHLLYG QIMQIPLPDI HHTEFLVLMG ANPVVSHMSL
CSVGRVAEEL HAIENRGGRV VVIDPRRTET AREHQWLPIL PDSDAWLLLS IINVLFAENL
VDRARVAKIA SGVESLRRLA TPFPPEATAE RTRIPAETVR GLARDLTQKR SAVYGRTGTC
LGSAPTLVNF LMDAVNILAG NIDQRGGVVF GEPVLPLVQL DAYTDAFSSY VPAKTRIGAM
PTVMGQEPAA FMAAEMTTPG PDQIRMLFVS AGNPVLSTPN GPELENALAG LDLMVSIDLY
VTETNQHADF ILPATAMYER EDLPVANGTF YLQPFVQATP AVVPPRGQAR LEAEILQEIA
EKAGVWPMPN PLVRLAAGVA NLVHLPVTPR RVLDTLIRLG RGGDRFGLRR NGLTLDRLIA
NHPHGVMFAD AVEVGRIRRV IRHRDKRIHL HHPEIRSEVQ RLGQRREDPD FSLRLIGQRE
PRSENSWMHN VAALRAARAP HAARMHPEDV DDLGLTHLGP VRLVSASGHI ELPVIATADI
SRGVVAVPHG WGHGGGSWKR ANREPGANVN ALASTNPADL DPLSGMSHLS GIRVRAERID
SVAPTGE
//
