ID A0A415CIV0_9BURK Unreviewed; 1037 AA.
AC A0A415CIV0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Molybdopterin dinucleotide-binding protein {ECO:0000313|EMBL:RHJ36150.1};
GN ORFNames=DW133_01665 {ECO:0000313|EMBL:RHJ36150.1};
OS Sutterella sp. AM11-39.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2292075 {ECO:0000313|EMBL:RHJ36150.1, ECO:0000313|Proteomes:UP000284958};
RN [1] {ECO:0000313|EMBL:RHJ36150.1, ECO:0000313|Proteomes:UP000284958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM11-39 {ECO:0000313|EMBL:RHJ36150.1,
RC ECO:0000313|Proteomes:UP000284958};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:RHJ36150.1}.
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DR EMBL; QRLV01000001; RHJ36150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415CIV0; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000284958; 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:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284958};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1037
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019015752"
FT DOMAIN 45..101
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1037 AA; 116395 MW; 8C6F49B7F4845327 CRC64;
MELSRRSFFK RSLLAAGSGS AVAFASGSAR AEADCLKKPY KLESVKEVTN ICCYCSGGCG
TICSSRNGEL INLEGDPDHP VNLGGLCPKG AAMWGLRNIV NPDRTVSAHP DRVIYPMVRR
PGSTKWERIS WDQAAKEIAR HVKKTRDASF VETEDGVTVN RCDGIASLGA AQLNNEEGWL
VQKFARSLGI VAIDNQTRVC HSSTVAGLAP SFGRGSMTSH WCDFANSDVI LTIGSNNVEN
HPLSSRWVER AQDRGATWIV VDPRYSRSAA QADIYGRLRP GTDIAFFGGM INYILQNELY
HKDYILSYTN AACLLRDDYK FDPDTGLFSG WDPVKQKYDN ESWGYDSDKK QLWNTAEGTA
FAWVNKPGTP KFKTPALKVL KRDETLQDPR CVLNVMKAHY ARYTPEMVER ITGMDHDVLL
KIWQTYAATG RPDKAGSILY ALGQTQHTYG SQNCRIMCVV QLLLGNVGIA GGGINALRGE
PNVQGSTDVG ASVHQAPGYL SWPTGKSHPT LADYLSVETY AAGYYSNKPK FWVSALKEWF
GDNATVENDY CYDLLPKISP RYDYAHYSTI MTFNQMRDER IKGYFCWGMN PAHSTPNAKH
ARNSMAKLDW LVVTDWFFTE TADFWRAPDM KPEEVKTECY FLPAALIYEK TGSINNSGRW
IQWREKSVEP PGEAKPDFDQ LLLLWREIRA LYEKEGGACP DQILKTNMDY TIDGKPDIRA
LCWAMNGYDV KTRKLIPSYG SLQADGSTAC GIWIFSGYYN NEATKMDPMK QPMTRRSKDD
PTGLGLFPQW SFAWPANRRI LYNRASADEN GKPWNPDRVL VEWKDGKWLQ NDVGDFVTAA
PPDRNAFFMT WEQQARLFAY PMGDGPLPEH FEPHETPVKN LLNGAGGNPC ALFTKDPSVK
RGNAKDYPYV VTTYSVVEHW QSGTQTRNIP WLNELIPCNF IEISEELAKE KGIQNGQMVR
VWNNRGDVKV AAMVTKRMKP MMIDGKVTHV VGMPHHFSWA TKFATGDNVN DLTPNVGDPN
SWIPEYKAFL VNLEPVA
//
