ID A0A101VSJ7_9FIRM Unreviewed; 683 AA.
AC A0A101VSJ7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=APF84_13400 {ECO:0000313|EMBL:KUO60027.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO60027.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO60027.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO60027.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO60027.1}.
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DR EMBL; LOEZ01000076; KUO60027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VSJ7; -.
DR STRING; 1734398.APF84_13400; -.
DR Proteomes; UP000053404; 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; cd02775; MopB_CT; 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 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.
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}.
FT DOMAIN 1..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 683 AA; 76248 MW; 4D6ECF952CCCCD64 CRC64;
MQITKHICPR DCYDTCGMIA HVDEYGRLVK VSGDPDHDYT QGKLCCKGYS YTQYVYHPQR
VTFPMIQEPR FSGNWKRISW DDALEIVARK MIELKNRYGS LLPMALVRGP GNYGVFTKSM
EFLLRSIGPF TLASGSLCIA AGWDAHLLDF GGVRYKNPTG MLNSNLLLLW GANPAATAIH
QMATIQKLRE HGGKVILIDI IPTATSLHCD EFIRVHPGGD GALALAILRQ MVIKNTVDYS
FIKDHSVGWE AFSSWLLQVD PQELINVSGV DEHKVEMIAD QIAESKPVSF WPGSGLQRYA
NGGQNMRAID ALVAASGNLY SKGGGLYFQN IDFWKLNHEI FSSAFSTKLY DPRLVGLNAL
AKELGACQNP PIKLMWFTSS NYLARGTDIL SMKKRIAEME LTIAVDHFLT STAAVSDIVF
PATTCFECQD LVAGYWHNKI GINQQAIEPV GECRSELKIS QSLSQMINHI EPGACSFPEE
RTSEEWFQSF TPWLKTNVEI SDYRELLNGA LPLQPPAEEK GNSCNIASGK YKFLTLEALK
QGCPEIPSLI NPMEPPSAYP YRFLVLHRAE HLNTQFSTVD WLQENILEEV CMNPSVAQRL
GIEEGDTVVI YNEIGEIQMY SKLDKDVPSD ILITYSWQDL FKKPVNVLTK VQETDLGQSL
TGFPGVAYHD TFVNLTRGKK GGG
//
