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Database: UniProt
Entry: A0A1Y4G9X4_9ACTN
LinkDB: A0A1Y4G9X4_9ACTN
Original site: A0A1Y4G9X4_9ACTN 
ID   A0A1Y4G9X4_9ACTN        Unreviewed;      1036 AA.
AC   A0A1Y4G9X4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Molybdopterin dinucleotide-binding protein {ECO:0000313|EMBL:OUO92145.1};
GN   ORFNames=B5F40_02115 {ECO:0000313|EMBL:OUO92145.1};
OS   Gordonibacter sp. An230.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=1965592 {ECO:0000313|EMBL:OUO92145.1, ECO:0000313|Proteomes:UP000196177};
RN   [1] {ECO:0000313|Proteomes:UP000196177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An230 {ECO:0000313|Proteomes:UP000196177};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUO92145.1}.
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DR   EMBL; NFJP01000002; OUO92145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4G9X4; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000196177; Unassembled WGS sequence.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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:UniProtKB-KW.
DR   CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
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; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 2.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..1036
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012282902"
FT   DOMAIN          46..103
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1036 AA;  115162 MW;  8009E4AC217AECFF CRC64;
     MGKLNLTRRT FAKLSAVTGA AIACATAAPH AALAEDATAS AKGGDVKRVR TCCRGCGKME
     CGVWVTVQDG RAVKVEGDQS SFQSSGNCCG KSQSSIQAAY HPDRIYHPMK RTNPKGEDPG
     WTRISWDEAM QIIGEKFNEI MERYGGQAIF NMCGTSRQWV YAPYCFYKWL FDTPNAHLAS
     EICKGPRRLM GWISSVDGAP WMALRDGPRV YVQWGTAPEN SNYDDSCRNL VDKMTEADVH
     ICIDPRLSGS GKEADYWLNL RPGSDGALAL AWQRIIIEHD LVDWEFVKRW TNASFLVVED
     MEPTGGRYFE LSSPMAGSTA GSPAPPADIA GTKLKTRLLK ESDVVEGGSP RKFYAWNKLA
     NGGAGGLVFW NTDTTQWEGC NHVAPTRDQM EVVYEGTSQE GYLPPLSYGE LVDAGIDLDM
     RESHEVTLLD GSVHTAKPVW AYLEESVADC TLEWCQEITG LDPALVEEAC LAWATRPEGQ
     TYGNGGIHLN LAPDQIGNCT QTVRAVIHLM YMTGNFDGPA GNRGLTRSPL DEQATSVPGS
     NMPQEVKAQL VALGTIPMEG VTPDPTNLPD KIDTLSNMIG AEKFPLTAYY NEWADATMIW
     EACINGDPYP LKGGINESGS FMNMSNATLA WEGLSKLDFW VDINMFHHPG TEMADILLPC
     QHWLEINNIR VSQGASGGIG ATVRCIEPPS DTKFDHDISR LIFDAVGGPN ATWNSLIDAT
     KPAPEHCDER MDEWFAVNSV ANSKVAWGSW QEFSDYYQEN GWINAKEIEP DRWGTYRRFE
     TGWMRMGKDA CTGKLFNCDN ETGEPVNNFG FPTPTALAEF WPMLFEAYAV DRANEFEPGK
     YDLIHEMLPH YDEPASGPKG DVDTSEYPII LTTGRRIPVY FHSEHRQLPW CRELWPAPRL
     ELNPEDAAEL GLEQGDWAWI ETEWGKVRQV VDLYYGIAKG WANAEHAWWF PELPAPTHGF
     TLSCIDCIWD PHGQDKHIGS SHMRGVPVKI YKATPENCPD GKVVPCAPED GTEIIYDASD
     PRLKEWLPNY EIREEA
//
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