ID C5B1L4_METEA Unreviewed; 726 AA.
AC C5B1L4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACS39648.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ACS39648.1};
GN OrderedLocusNames=MexAM1_META1p1806 {ECO:0000313|EMBL:ACS39648.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS39648.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS39648.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001510; ACS39648.1; -; Genomic_DNA.
DR RefSeq; WP_012752628.1; NC_012808.1.
DR AlphaFoldDB; C5B1L4; -.
DR STRING; 272630.MexAM1_META1p1806; -.
DR KEGG; mea:Mex_1p1806; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_5; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000009081; Chromosome.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
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; 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.
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 Oxidoreductase {ECO:0000313|EMBL:ACS39648.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT DOMAIN 21..78
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 726 AA; 79869 MW; FA006865F7D61764 CRC64;
MLEERISEID AEAAAKSVSE AVTRLGACPH DCPDTCSMIY TVENGRLIDV RGNPDHPMTR
GALCGKLKDF DRHHYNPDRI LYPMRRTGPK GSGQFERIGW DEALAEIHRR FTGIIETHGA
EAILPYNYLG NEGVVQGLTV GDAFFNRLGA TVAEKTFCGS GSCTAWLLTV GPTNGTDPMS
FAQSKLIVIW GCNSVSTNIH HWHVVKEAQR HGARVIVIDP YRSRTAAQAD WHLMPKPGTD
GALAMAMIHV IIEEGLTDDD YIARHTVGFE PLKERAQAFT PEYAAEICGI PADDIRQLAR
EYATTRNAAL RPGVAVERSA GGAQALRAIF SLPALTGSWK DPGGGVYQMP LWEFPVHWDR
VCRPDLIPEG TRVLNVLKLG EVLTGEAGIE PGIHALMVYN ANPVSNSTET AKIKRGLARE
DLFTVVSEHF VTDTARYADI LLPATMAAEH DDMMFSWGHF FFTLNQKAIE PPGETVANAE
LFRRLAKTFG FTEPQFSMSE TELMEWYLDW ESPKLGGIGM DHFRQHGWYR LNIGDPDTRT
PHAEGNFPTP SGKCEFYSEA AVTSGNFVAP PFRQMYEQFQ GGEALDPLPG YVPANERPET
NPAQAERYPL NIVSPKSHGF LNSQYANEAH KVRAQGEQTI LINPADAQSR EIGEGALVRV
FNDRGAFHGQ ARVTEEVPPG LVIASLGYWH SLNRDGAVNV ISASTYGGMG HSPTFSDNLV
QVGLAQ
//
