ID A0A0Q0VPQ3_9BACT Unreviewed; 1151 AA.
AC A0A0Q0VPQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Molybdopterin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=APR54_03285 {ECO:0000313|EMBL:KQC10157.1};
OS Candidatus Cloacimonas sp. SDB.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC10157.1, ECO:0000313|Proteomes:UP000052007};
RN [1] {ECO:0000313|EMBL:KQC10157.1, ECO:0000313|Proteomes:UP000052007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC10157.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:KQC10157.1}.
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DR EMBL; LKUH01000155; KQC10157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0VPQ3; -.
DR Proteomes; UP000052007; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00368; Molybdopterin-Binding; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12837; Fer4_6; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 615..645
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 658..687
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 696..752
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1151 AA; 130416 MW; 0AC1041B4C15B63E CRC64;
MITVKLNGKE VKTNPGKTIL EVAEENDLII PTLCHDKELE PFGSCWVCAV KVEGRKGFVT
ACGTKIVDGM NITTDSEEVY SARKMALELL LSDHYADCEA PCKIACPNHL DVQTYVSLIA
NGQYKESLQV IKETLPMPLS IGRVCPAFCE DECRRKLVEE PIAIRQLKRY VADLDIEDEN
PFIPEKEAPK NEKIAIIGAG PSGLTCGYFL SNKGYNVTVF EAAEKAGGWL RYGIPEYRLP
KKVLDKEIKL MCANGMKIKT GIQIGKDMTL SELSSKFDAV FLAIGAQNAV PMKLKGNDLN
GCFLGVDFLK DFVLGNKIKI GKKVMVVGGG NTAIDCARTA RRLGSDVTIV YRRTRKEMPA
ETYEIDAAEE EGIKFHFLTN PVENFGQKGK LVSVKLEKMK LGKPDASGRR RPEPTGEFFK
EDFDTMIAAI SQVSEINFLA DKANKIDGKE IPLTRWSTAI IDEETMHVGI KNIFAGGDFR
RGPATAIEAI YDGRIAAEAI DRYLRKEMLM DPVVLFDSKK EKKLKDVDPA HYKQYKRINR
FKMPELEPEA RNTNFLEIEL GFSNEDATSE ASRCLECGCQ VNQTCKLREY ATEYKIEVEL
FKGDKNKHPI DETHPFILRD PNKCIKCGRC VRICAEVQGP GVLGYIYRGF TSYVAPEFGE
SLTKTTCESC GKCIEVCPVG ALLPRNLNYK LNPHPLEVVE QNCGLCGTGC EIRIQVQTDK
IAYINPAGNE KLNDRNLCFD GKFGWQMLES DDRPITSYVR KEDTIDEVEE SWVESNDFTE
ISQLIKNKLN NAKTRKIYVA PNATNEEILL MKTVAEKINA EIASLSYQKC FMSDLKNTVL
MDKTYDDIKQ AEVIIIVGKI SSVLKTMIRN EQRKGKKLIL INNNHEEFNR FADELYNEDP
ITDTLDRILE NYYEEDEDME ENDTDSDSET ILPLELNVPA KTLFLYCREN VSEEVAWNIW
MLSSLICDFK AGSGVLQTSQ FCNLKGLNRF GILPGKPQNS DFVIFYKELP CEEQKKLLKN
SKFMISINTH IDESDPSHIF IPAPSYLEIE GSAIANDGRI TSFKNPKKSR IFNNLLIKLY
DLNLIDEEQS DPIYWLKEVK KELKKVEPKR EMTDQQLLDY LYTLEDIKFN IPKLHNVQKI
RLDTMKKLLR Q
//
