ID A0A0K2YM39_9NOCA Unreviewed; 710 AA.
AC A0A0K2YM39;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CRK53991.1};
GN ORFNames=RHCRD62_70285 {ECO:0000313|EMBL:CRK53991.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK53991.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK53991.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK53991.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CVQP01000010; CRK53991.1; -; Genomic_DNA.
DR RefSeq; WP_050066916.1; NZ_CVQP01000010.1.
DR AlphaFoldDB; A0A0K2YM39; -.
DR STRING; 260936.RHCRD62_70285; -.
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; PTHR43105:SF14; POSSIBLE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE 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 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 5..61
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 48..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 75353 MW; 895F79D434792B65 CRC64;
MRSATSRRTS YCRLCASSCG VLLDVEDGRI ARVLGDAHHP ISGGYTCPKG RRGGDLVHGP
DRLTTSMRRT PDGSHEPVPV SRAVTEIAAR LRTVVDRHGP DAVALFMGTQ QNFAALTPPM
VRAWFKGTGS HKLFSTMTID QSAKWVVAER MGTYLGGRQR FEDADVWLLA GTNPVVSGNG
GDGDGAVVQN PSVTLRAARE RGLQLIVVDP RRTETAALAD VHLAPRPGTD AVLFAGLLHV
VLTEGLHDDE FCRRYTADLD LLVDAVSVVT PAVVQRVCGV SADLLRHAAR VFAGGRRGMA
TSGTGLCMGP HSNLAEHLVA ALNVVCGRYL REGERADDRA VLTRYVPARA EVAPPSRSYE
HGYRSRIGGV RAIRGELPSG ILADEILDPG PDRIRALVVS GGNPAAALPD RAKALRALRS
LDLLVCVDPR MSDTARLADY VIAPTVMYER ADHTAIMEPF FPRRFAQFTP PVVTPPPGVV
DDWRFFLDLA AASGQPVKFA GRILDPAAPP TSEQLLAMTA ERGRVPFADL VTARHGQLAG
DSGALVGPPD PGAAGHRLVT MPDDVRAELG AALTEVTVTQ RFPMLLTVRR IREAVNSTGT
RVPGLVRGGT NPASMHPDDL AALGVADGQQ VTVHSASGRL RATAKADPTL ARGTVSMTHC
FGSVDPGDDV GVNVNALTGT RDGVQTINAM PTMTAVPVTV GPAAPEEESR
//