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Database: UniProt
Entry: C1AZB6_RHOOB
LinkDB: C1AZB6_RHOOB
Original site: C1AZB6_RHOOB 
ID   C1AZB6_RHOOB            Unreviewed;       709 AA.
AC   C1AZB6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAH50044.1};
GN   OrderedLocusNames=ROP_17970 {ECO:0000313|EMBL:BAH50044.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50044.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH50044.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH50044.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH50044.1; -; Genomic_DNA.
DR   RefSeq; WP_012689002.1; NC_012522.1.
DR   AlphaFoldDB; C1AZB6; -.
DR   STRING; 632772.ROP_17970; -.
DR   KEGG; rop:ROP_17970; -.
DR   PATRIC; fig|632772.20.peg.1885; -.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000002212; Chromosome.
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   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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}.
FT   DOMAIN          5..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   709 AA;  74464 MW;  4E9D9F7C9069B6FE CRC64;
     MRSVTSRVTS FCRLCASSCG VLLDVEDGRI ARVLGDAHHP ISGGYTCPKG RRGGDLVHGP
     DRLTTSMRRT AAGTHEPVPV AGAVTEIAAR LRTIVDRHGP DAVALFMGTQ QNFAALTPPM
     ARAWFRGTGS HKLFSTMTID QSAKWVVAER MGTYLGGRQR FEDADVWLLA GTNPVVSANG
     GDGDGAVVQN PSVILRAARD RGLRLIVVDP RRTETAALAD IHLAPRPGTD AVLFAGLLHV
     VLTENLHDAD FCGRYVADLP ALAAAVVGVT PAVVQRICGV PADRVRDAAR VFAGGARGMA
     TTGTGLCMGP HSNLAEHLVA ALNVVCGRYL REGERADDRA VLTRHVPARA EVAPPTRAYE
     HGFRSRIGDV RAIRGELPSG ILADEILEPG PGRVRALIVS GGNPAAALPD RGKALRALRS
     LDLLVCVDPR MSDTARLADF VIAPTTMYER ADHTAIMEPF FPRPFAQFTP AVVPPPPGVV
     DDWRFFLDLA AASGQPVKFA GRILDPAAPP TSEQLLAMMA ERGRVPFADL VAAPHGHLAG
     DSGAVVGPAG KEGAGHRLVL MPGDVRGELR AALTDSPVTP QFPFLLTVRR IREAVNSTGT
     RVPGLVPGGT NPASLHPDDL AALAIADGQA VTVRSASGRL RATARADGTL ARGTVSMTHC
     FGGVDPRDDV GVNVNALTGT GDGVQSINAM PTMTAVPVTV EPTATEQDV
//
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