ID A0A0Q7AS55_9BURK Unreviewed; 683 AA.
AC A0A0Q7AS55;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:KQW38589.1};
GN ORFNames=ASC76_11355 {ECO:0000313|EMBL:KQW38589.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW38589.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW38589.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38589.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW38589.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38589.1,
RC ECO:0000313|Proteomes:UP000051611};
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 -!- 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:KQW38589.1}.
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DR EMBL; LMDS01000004; KQW38589.1; -; Genomic_DNA.
DR RefSeq; WP_056465539.1; NZ_LMDS01000004.1.
DR AlphaFoldDB; A0A0Q7AS55; -.
DR STRING; 1736528.ASC76_11355; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000051611; 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 CDD; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 1.
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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR037920; YoaE_C.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 683 AA; 74614 MW; 35730BAEBF9F1270 CRC64;
METITVRAAC PHDCPDTCAI RVTVQDGRAI KVQGDPDHPP THGALCTKVS RYPERTYHPE
RVLHPLRRVG PKGSGRFERV SWEEALTDIA ARLRTIAARD PQAIVPYSYA GTMGLVQGES
IAARFFHRLG ASLLDRTICS SAGGEALAST YGGKVGMHLE FFAESRLILI WGSNSIASNL
HFWTFAQAAK RAGAKLICID PRRTETADKC HQHIALLPGT DGALALGLMH ELIVNDWLDD
DYIARHVDVA GWPALRERAL EWPPERVAEV CGITADEVRG LARDYGTTRP AAIRLNYGMQ
RVRGGGNAAR LVALLPCLTG AWRHRAGGLL FSSSGWFRSV RNDAGLQRPD LLAGRAVRTI
NMSTIGDDLL RESSADFGPK IEALVVYNSN PVAVAPESPK VVRGFARDDL FTVVLEHFMT
DTADLADYVL PATTQLEHLD VHTSYGHTWV MLNEPAIAPV GESKPNTQIF RELAARMGFD
EPCFADDDEA LARAAFHAPV DFDALREHGW FKLPVADAPF AEGHFPTADG RCIVDSKLHG
VPDHVPNYEA VLSAPALARR FPLAMISPPA RNFLNSSFVN VTSLRDIEGE PLLEIHAADA
QGRGVVDGAM VQVFNDRGRY LCRARISPRA RPGVVNGLGV WWRKLGAGGS NVNEVTHQQL
TDIGRAPSFY DCLVEVRPAD AVS
//
