ID A0A0Q7YYC5_9SPHN Unreviewed; 707 AA.
AC A0A0Q7YYC5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=ASD67_18765 {ECO:0000313|EMBL:KQZ61285.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ61285.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ61285.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ61285.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ61285.1}.
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DR EMBL; LMGF01000005; KQZ61285.1; -; Genomic_DNA.
DR RefSeq; WP_056350440.1; NZ_LMGF01000005.1.
DR AlphaFoldDB; A0A0Q7YYC5; -.
DR STRING; 1736474.ASD67_18765; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000051141; 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 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 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 707 AA; 75763 MW; AEE8EFF14C0D735B CRC64;
MPEVRRSFCR FCHANCAMLV TIDEGRVTKV QGDPDDPVFG GYTCIKGRQL PEAHHGPQRL
TVSRKRVDGA FQDIAMETAL DEIGARLSAI IAEHGPHAVA VYGGTYAFQN SAGVGSAMAF
AQGLGTRNIY TSVTLDQPAK VYTTMRYGNW MGGMHTFAEA DVAFFIGNNP IVSHYGPPGG
LPPFSPSRRL RDALDKGLKL IVADPRESDV AALAHIHLPV RPGEDPAMLA GIIHVILSEG
LYDKGFVQQY VDGLDDLQRA VADFTPAVAA ARAGVDEAQL VAAARMFATG TKGVVSTGTG
PEMAGQGTLT QYLVSSLNIL CGRFCREGEK SSIPRVFTAV SPRRAQVSPP MALYGEGFPA
SRIRGLTHLG MEMPCNVLAD EMLTPGEGQI RALIVIGGNP VVAFPDQDKM TRALGGLDLL
VCIDVNAESA TAKRSDYILA PTMCLEREDI SNLSEWWYEI PYARYTEAMI DAPGDLIEEW
EMLWGLAHRI GSPIPLAGGP CPMDEKPSKQ TFLDLMTAGC VVAPGQVRAD TVDGQAVIYP
DLHPIVEAGD PDAPGRFDLC AGAMPDQLIA YATADQPAPD FPYRMVSRRS RHRFNSTGQN
LPALTAKRTT NPAFLHPDDM ARIPCSEGDI VRIRSAAGEV VAEARAATGM RPGVVSMAHA
FGGPDVGPDE VRTRGNSTNR LVSESVRYDP ITGQSLQSAI PVAITPA
//
