ID A0A1Q6W963_9GAMM Unreviewed; 685 AA.
AC A0A1Q6W963;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Molybdopterin-binding oxidoreductase {ECO:0000313|EMBL:OLB09633.1};
GN ORFNames=AUH10_14045 {ECO:0000313|EMBL:OLB09633.1};
OS Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB09633.1, ECO:0000313|Proteomes:UP000186999};
RN [1] {ECO:0000313|EMBL:OLB09633.1, ECO:0000313|Proteomes:UP000186999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLB09633.1}.
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DR EMBL; MNCZ01000133; OLB09633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6W963; -.
DR STRING; 1805166.AUH10_14045; -.
DR Proteomes; UP000186999; 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 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 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..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 685 AA; 73640 MW; 817AE9BD140FDB00 CRC64;
MNVQKPSVCP LDCPDTCSLA VTVADGEVLA VRGTKANPIT HGAICAKVAR YYPQFVHGPN
RLRHPLERIG AKGEGRFRQT TWESALELIQ RRVGAVIERY GPEAVLPLNY AGPHGMLAGD
SMSLRFFHRL GASLLARSPL CGGIRSAAYA ATFGATPGTP LQQVALAQLI IVWGNNASAC
NLHLMRQINA AKRHGARLVV IDPRRTQVAE QAHLLLPVRP GTDVVLAWAI ATELERISGL
DQEFIGRHVL GFDDFMRAAR AYPPERAAEI CGVGLDDVRT LARWYKESTP AVIAWGNGLE
RNRNGGSGLR AIAALPALAG KFGVPGGGLV GGASHAFPKT LDRLTRPDLA PPGTRTINIL
DVAESILDEQ LTPPIKAVFV YNHNPIIVHP DQNRMRKALA RDDLFTVGIE VAMTDTMAFA
DVVLPACTHF EHADLYPAYG QQYLQRAEPV IPPVGESLPN TEIFRRLAAR FGFSDPAFTA
SDAELMDAAM NADDPRLKGR RPSQLPLDSA LKMEYGGVEP VLCDTVWPRT PSGRIELVSE
TLRARHGAPL PGFRPLQSSY PLTLITPASD KRITSTFGGL PASDGTPVLE MHPEDAAARG
LKEGELAKVW NDQGEVFLPL QITPAVRPGV VCSEKGAWLR TSLNGQTVAA LAPTHKADIA
DGACFNDTRV EVQAAQPSAP AGPGS
//
