ID A0A126ZHR7_9BURK Unreviewed; 1155 AA.
AC A0A126ZHR7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Ferredoxin:oxidoreductase FAD/NAD(P)-binding protein {ECO:0000313|EMBL:AMM25981.1};
GN ORFNames=AX767_17690 {ECO:0000313|EMBL:AMM25981.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM25981.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM25981.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM25981.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014517; AMM25981.1; -; Genomic_DNA.
DR RefSeq; WP_068632520.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZHR7; -.
DR STRING; 1795631.AX767_17690; -.
DR KEGG; vaa:AX767_17690; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000070169; Chromosome.
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 CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd02759; MopB_Acetylene-hydratase; 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; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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; IPR041930; Acetylene_hydratase.
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:UP000070169}.
FT DOMAIN 3..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 807..924
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1073..1155
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1155 AA; 124996 MW; 6266EBF961C1ECCC CRC64;
MAIEEKQGYC TLCRSRCGTL NAVENDRLIA VRPDPSHPTG QAMCMKGRAA PELVESPHRL
HYPMRRTRPK GDSDPGWVRI GWDEALAETA QRLGAIRAES GAESVVFAVT TPSGTPLSDS
IDWIERFVRL FGSPNICYAT EVCNWHKDFA HAFTFGCGMP PADYANAELI VLWGHNPANT
WLAQAHAIGR GRARGAKMVV IDPRPTALAN QADVWLPVRP GTDAALALGL IHLLIADDRF
DHAFVREWTN APLLVRSDNG LFLRERDLWP RAASNRYMVW DDARQGPVPF DAEVPADAQG
ADNFRLRGEV IVALAEGRAG AQSLPCAPAF EWLAQAAAAY TPAEVQRITG VTEVPLRAAA
TFFGEGRRVA YHAWTGIGQH TNATQAERAV ATLYALTGSF DTVGGNRVRT PPETRSINPL
SLLSEAQRAK ALGLEERPLG PPAHGWVTAR DTYRAILDGK PYPVRAMMAF GTNLPVSQAD
TAMAHEALRA LEFHVHCDLF ETPAAQYADI LLPINTPWER EGLRMGFEID DAAAARVQLR
QQMVTTRGES RSDNDIVFDL AVRLGMGGDF FGGSLEAGWD HMLAPTGLSV AQLRAQPAGA
NCAIDVRERK YALPDAQGRL NGFDTETRRV ELYSERLLRH GQPPIARFVE PADSPRDAAA
TRGGRYPLVL SSAKNGLYCH SQHRSLVSLR KRAPDPVVEL SPALAAARQI AEGDWVRITT
RTGAARFVAR LVPGLADDVV VAEFGWWQAC PELDREAQPV EGALGSNFNA MVSADASDPV
SGSVPHRSFL CDIARDPATE ARQRRWPGWR PFRVSALQAE ADGVLGITFE AVDGGLLPDY
RPGQHIELQV QPSAGAPAVT RAYSLTGAAV VPERTHYRIA VRHQRGRTAD GAPYEGHVSG
HLHRALQVGD VASLRAPSGG FVLPRVSPQP LVLLAGGIGI TPFLSLLESL PDGADGPEIW
LYGANQNSAT HAFRQRIAEH AARLPCLRVT DHYSAALPHD RAGVDFASQA LVDASVVSDA
LIARRARFYL CGPAPMMDAL VAGLVARGVP RFDIFSEVFR SPAAPTLVGD QRFAVRFARS
GGAPATWSPA EGTLLTFGES LGRAMPSGCR VGQCESCAVR LLSGRVRHLH GTEPADPDTC
LTCQAIPLED IVLDA
//
