ID G9XP77_DESHA Unreviewed; 669 AA.
AC G9XP77;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:EHL06505.1};
GN ORFNames=HMPREF0322_02775 {ECO:0000313|EMBL:EHL06505.1};
OS Desulfitobacterium hafniense DP7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL06505.1, ECO:0000313|Proteomes:UP000004416};
RN [1] {ECO:0000313|EMBL:EHL06505.1, ECO:0000313|Proteomes:UP000004416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP7 {ECO:0000313|EMBL:EHL06505.1,
RC ECO:0000313|Proteomes:UP000004416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHL06505.1}.
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DR EMBL; AFZX01000070; EHL06505.1; -; Genomic_DNA.
DR AlphaFoldDB; G9XP77; -.
DR PATRIC; fig|537010.4.peg.2601; -.
DR HOGENOM; CLU_000422_13_3_9; -.
DR Proteomes; UP000004416; 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 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..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 669 AA; 73489 MW; 85819954D8FA7D0D CRC64;
MVKTSICCLC NGGCGLKVHI GPEGTIKAIY GDPDNPYNKG KICPKPIEII ENLRGPERVQ
YPMKKVNGEF VRISWEEAID TIAKKYKEFS DNFGTGSVIG ITSKIGGSFS KFALKIFGEI
AGFANYGTGP ICFSSEEKVR KEMFGKAAAS APLHDVIYSK LVLNVGNNCA QTKAGQFHWL
QEGQKHGAKI ITIDTRYTET AQLSDQFIQV NPGTDAALGM ALLHLVIKHK HYDEEFVRDQ
VNGFAELAQA VEDFTAEKAA AITGVPEKVI EELAYELGTK KPAIMWPGRG IVMVNNGEQA
LMAFESLFAI LGNVGKPGAG VVSHINGYGQ PADLIKPEHV VKPSFKLPAD KVIEGMETGQ
IKMIYIAGNP CANWPESARM KKALGKLDFV VSHTLTLDDS ACLAHIVIPA THWLEEAGMQ
PGIHRVMQWR DKAVEPYGES KPAAEVFKLL AAKMGLPTEY FADTPEEAWD MERRHIAGIS
AITVAKMQEK PGGVHYPYPE GGEESHRLYS KGFNTPSKKV ELLRGKGSVL HYKDPLQSPG
NEGLSIEDYP YFISSVKVAA HYHTQCQYSR LAREFEKPYV EVHPQTALKL GVKDGEAIRI
ETPAGAISLP AKLTYSVPQN HFFTQPYFSK RYNSDSINTL LPSVLDQPGG NFPHKNVLCR
AYSEGGCKK
//
