ID A0A5J5FT16_9GAMM Unreviewed; 1132 AA.
AC A0A5J5FT16;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Molybdopterin-dependent oxidoreductase {ECO:0000313|EMBL:KAA8995632.1};
GN ORFNames=FJU30_24035 {ECO:0000313|EMBL:KAA8995632.1};
OS Affinibrenneria salicis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Affinibrenneria.
OX NCBI_TaxID=2590031 {ECO:0000313|EMBL:KAA8995632.1, ECO:0000313|Proteomes:UP000335415};
RN [1] {ECO:0000313|EMBL:KAA8995632.1, ECO:0000313|Proteomes:UP000335415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L3-3HA {ECO:0000313|EMBL:KAA8995632.1,
RC ECO:0000313|Proteomes:UP000335415};
RA Li Y.;
RL Submitted (SEP-2019) 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:KAA8995632.1}.
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DR EMBL; VYKJ01000018; KAA8995632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5FT16; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000335415; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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 GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.30; -; 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; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000335415}.
FT DOMAIN 3..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 788..903
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1052..1132
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1132 AA; 123701 MW; F4F93CA0A7F0E85E CRC64;
MSTVNRPGYC TLCTSTCGAI YSIENDRIVS IRNDADHPTG GAMCLKGKSA SELIDNPERL
THPMRRTNPK GSKDPGWAAI SWDEALDEIA GRLLAIKAQS GAHAVAFGIT TPNGTPIADS
SEWIERFIYT FGSPNICYAA EICNWHKEIA HSFTYGCGMP APDYLNSDLI VLWGHNPTNT
WLAQAHSIGE ARKAGAKLIV VDPRDTALAR EADVWLRIRP GTDAALAMGL ANAFLESGAY
DRSFVHQWTN GALLVRTDTG RMLRGAEVGL TLDNAYVYFD RTTQDLQPHL AALAGGCIPD
AAQLNVEQSI TLVSGEQVKC ASAFTLYRRA CLPFDMEKTA QATWIDADKI EQAATLIASS
QRISLHSWTG VEQHNNATQS QRAISCFYAL TGCFDAQGGN RIFGSLKSVT VNDLSLLAPE
QLEKALGYRD RPIGPSANGW VTSRELYEAI LNADPYQIRA LVSFGGNLLL AQSDRQMAER
SFEALEFHVH CDLFINPTAE YADIVLPVNT PWEREALRIG FAITTRAQEW VQLRQQMVSP
RHDTRSDTDI VFALAGRMGM REEFFGGDKE AAWNAMLAPL GLTTGQLRQQ PAGVRIPIEH
ATEKYRLTGF NTASGLIEIY SESLHVRGYA ALPGFEAGDI IQPNEAYPYV LSSAKSGYFC
HSQHRQLAGL RKKSRNPTLE LSQQLAAELH IADLDWVIVT TRTGQARFQA RVNPNLHPRV
VFGQHGWWQP CIPLGASGMP VSGPQNSNYN GLIDADEKDP VSGSVPLRAF TCSLRREDQT
LLAPGRWPDF RDFYVSEMVA EANGVHRVHL RPLDNSLLPG FDAGQHITIR VTLRSGMVVS
RAYSLVGIAS ERPVEQYAIC VRNSQADDVD EPLQPSVSHH INRHLAPGDR VGVQAPGGNF
TIPCQAGRPL VFHAGGIGIT PFMTVLETAA LAQSKTRMLL IYGNRNSAAH VFRLRLKQLK
AQLPGLEIID VYSRPLPSDQ PGVDFNYQGY VDCSMIPEAF TTGRPLHYMC GAESMMSAMT
SQLIASGVPK ADIFKEAFKS SVNISAVAAG EFDVNFARSN KTIRWTSQCG VLLDFATANG
ITLASGCRVG QCESCAVNVL DGRVLHLQGN PDEDNVCLTC QAIPGSDITL DA
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