ID A0A0K2YQY0_9NOCA Unreviewed; 706 AA.
AC A0A0K2YQY0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CRK53994.1};
GN ORFNames=RHCRD62_70288 {ECO:0000313|EMBL:CRK53994.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK53994.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK53994.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK53994.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQP01000010; CRK53994.1; -; Genomic_DNA.
DR RefSeq; WP_050066919.1; NZ_CVQP01000010.1.
DR AlphaFoldDB; A0A0K2YQY0; -.
DR STRING; 260936.RHCRD62_70288; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000044872; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 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:UniProtKB-KW.
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:UP000044872}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 706 AA; 77747 MW; 884055EB5201E1A5 CRC64;
MTRTVHTFCR ICEPGCGLLA EVDGGEIVRL RPDADHPVHK GFSCHKGVHY LQVHRDPDRL
DRPLKRMNPR TEDGGVFEPV GWDDAARDIA ARLADIRRRH GRNALAVYQG NPSAFNGAYY
ANAATIARGF DTRMRFSAGT QDTSAKYAAS EAIYGASMAH PIPDLLHTDY FLCLGSNPQV
SHMTLIHISD PMAKIRAINR RGGTVLFVNP RRIESSSPET GDVLMVKPDT DFYFLAGLLH
EIVFRIGFDR AAVERRARRV DELLDFVRQY PVDRVASVVG VPAAAIRRVA DEFCAAPSAS
IYMATGVNQG RQGALAYWML TMVSLFSGNL GRRGGNIYSR GVADTVQHSK RKREDPFFEG
PFGEMRTVGG DLPAALLPDF IENADDPIRA LIVVSGNPLL SVGGDDRLRR AMQSLDLIVT
VDLYRTVTGE IADYVLPATD WLEREDVNFL NTMGVAMEPY VQYTPAVVPA RGERRDDWWI
LSRIQQEMGV PGLLDDPEPN PLAAVDSVLR ESGLTIDRLK GMSCQTAVLP EAVPSDVFDI
AVQHEDGLID CCPALFRRSY ATVESIFGEL AAEPADQLKL ITRRTNYMVN SWLHNIPVLK
QGVHQGNPLW MNPDDARGRG LVEGDDVAVR SRHGEVDAVL AYDPALRSGV VAMTHGWGQG
TARGLDVARR HPGVNVNRLA PTGAEGYDPL SNQSQLTGIN VDVLRR
//
