ID A0A143BKT0_9BACT Unreviewed; 1013 AA.
AC A0A143BKT0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Molybdopterin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GEMMAAP_10560 {ECO:0000313|EMBL:AMW05141.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05141.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW05141.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05141.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW05141.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05141.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP011454; AMW05141.1; -; Genomic_DNA.
DR RefSeq; WP_026849778.1; NZ_CP011454.1.
DR AlphaFoldDB; A0A143BKT0; -.
DR STRING; 1379270.GEMMAAP_10560; -.
DR GeneID; 78444576; -.
DR KEGG; gph:GEMMAAP_10560; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0437; Bacteria.
DR OrthoDB; 9789030at2; -.
DR Proteomes; UP000076404; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10551; PsrB; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF13247; Fer4_11; 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; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 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:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 748..778
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 827..858
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1013 AA; 107760 MW; 233DE26F926CF1C4 CRC64;
MSTEAGTGVK RRDFLKILGA TSATTAVVGC SSEKVGKLIP YVASPDNTVP GVSQYYATTC
RECAAACGVL AEVRDGRPIK LEGNPDHPMN RGAICATGLS AMQGLYNPDR YRSPMVREGN
ALKPTTWDKA YELLAQKLGE VKSKGQAGSV VFINQHESGT FPGFLDQWLS ANGMPNHLSV
DSTAPVATIA ANQKAYGAAW PQLDFGAAKL VISFGADFLD GWGHSVPQQL DWADARAKLT
DAPRLVYVGA RRSLTGLNAD QWVPAKPGSE MALCAALTGA GTAQAASDAS GVSVATIEAL
AKAIAEAGNG VMAICGVTGA DAVECATMVA EINKKAGAVG TTIKPANAHA GYNGLASYAD
LATAVKAMDA GSVPLAFVRG ANPAHSMPKS AGFAAAFAKV GFKVSFSAMP DETAQLADLV
LPDNHWLESW GDAAGANGQL GLQQPTLDPV FDTRSTADVL IEMAKKDQAL AARYNVADYR
TWYISKFPGG GSAFTTALTK AQVSSSPLVP TSSRALSAAA QAPAAGTGDF FVHVFPSPTL
GDGAGANKPW LQELPDPVSK IAWQSWVEVH PSTAKKLGIK EGTHLTVETA AGKVTAPAYI
YMGVRPDTVG ISLGLGHTAY GRFAQNIGVN AYDLVSTGWD AAGGLALGNI KGKVTVTADN
SPLVTTEGSA RQHGRGIGQA LPIGVLLGTE QEDAEHHHEI PGLPSQDFKA GLKSPVAADA
QGEFANPESK DKGMYDPNHS SKAEKRRWAM TIDLARCTGC SACVTACYSE NNIPTVGAPY
QGRALSPTNW DERPGANIIK GREMAWIRLE RYYEGNNNTE NEFSPDFDTR FVPMMCQHCG
NAPCEPVCPV YATYHSPDGL NVQVYNRCVG TRYCSNNCPY KVRYFNWFGY GEPERRQYAW
PEPMHWSLNP DVTVRGKGVM EKCTFCVQRI RESEHRAKAE GREVNADEFT TACAQACPSR
AIVFGDAADE NWTVSKLAYD RRAYHVFEEL NTYTAVVYLK KVTYPSPASP ATA
//
