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Database: UniProt
Entry: A0A3P0X771_9BACT
LinkDB: A0A3P0X771_9BACT
Original site: A0A3P0X771_9BACT 
ID   A0A3P0X771_9BACT        Unreviewed;       745 AA.
AC   A0A3P0X771;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:RRA47927.1};
GN   ORFNames=D1Y84_06115 {ECO:0000313|EMBL:RRA47927.1};
OS   Acidipila sp. EB88.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidipila.
OX   NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA47927.1, ECO:0000313|Proteomes:UP000279598};
RN   [1] {ECO:0000313|EMBL:RRA47927.1, ECO:0000313|Proteomes:UP000279598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB88 {ECO:0000313|EMBL:RRA47927.1,
RC   ECO:0000313|Proteomes:UP000279598};
RA   Pold G., Deangelis K.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RRA47927.1, ECO:0000313|Proteomes:UP000279598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB88 {ECO:0000313|EMBL:RRA47927.1,
RC   ECO:0000313|Proteomes:UP000279598};
RA   Horta L.;
RT   "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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:RRA47927.1}.
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DR   EMBL; QWEV01000005; RRA47927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P0X771; -.
DR   OrthoDB; 219031at2; -.
DR   Proteomes; UP000279598; 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   CDD; cd02766; MopB_3; 1.
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   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000279598}.
FT   DOMAIN          3..62
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   745 AA;  80961 MW;  B96FAD928B6AF1CE CRC64;
     MATHTRRSVC SLDCPDSCGV LVTIDTETGE ALRVAGDPEH PVTRGFLCGK VAKYLDHVYA
     PDRVLYPMRR RAGVPKGPLA PGAQNAAFER IGWDEALHAI ATRLGAIARE RGPEAVLPYS
     YAGTIGTLGY GSMDRRFFHR FGASQLKRTI CATAGGEAFL SVYGRKLGTD TEHFHHARLV
     IAWGANIHNN NIHLWPQVEE ARRNGAWLVV IDPYATRTAQ LADQHLAIHP GTDTALALGL
     MHVILRDGLE DAAWCEQHTH GLAELRAHVR SYTPAMVEDA TGIAANLVEE LARAYATTKP
     AVIRLNYGVQ RSENGGAAAR AVCMLPALTG AWQHLGGGLQ LSTSGAFSFD SQAVERPDLM
     YASPLGRAAR TVNMAQLGDA LCDLEKPAVH ALFVYNSNPA VIAPEQRKVL RGLQRDDLFT
     VVHEQSFTDT CDYADYVLPA TTFLEHVDMQ GAYGHYYVQL SEQAIAPVGE ARANVELFSA
     LAQHMGYTES CFSDDAETLI AQALREDAAP EDTTPGSVLM RGITRATLRA HGGSERLHFP
     SEHAVAPEPF RPFSDGVFPT PSGKAEFFSE QLAAQGQDAM PTYHPPVELR TRQTPADAEG
     MLQFLPRKSG NFMNSTFANH AAHQKMQRET LDLLELHAED AQVRGLAEGD LAEIRNERGA
     LRLRVRISRR VQPGVASAGM AWSKLNPEGG KGVNQLTSQR LTDLGDGPTF YSTLVQVRRV
     QCACEAETGC VLCHVGALEA GVSLE
//
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