ID A0A0S8A134_9GAMM Unreviewed; 737 AA.
AC A0A0S8A134;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=AMJ53_09625 {ECO:0000313|EMBL:KPJ92313.1};
OS Gammaproteobacteria bacterium SG8_11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703402 {ECO:0000313|EMBL:KPJ92313.1, ECO:0000313|Proteomes:UP000051175};
RN [1] {ECO:0000313|EMBL:KPJ92313.1, ECO:0000313|Proteomes:UP000051175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_11 {ECO:0000313|EMBL:KPJ92313.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ92313.1}.
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DR EMBL; LJNJ01000175; KPJ92313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8A134; -.
DR PATRIC; fig|1703402.3.peg.629; -.
DR Proteomes; UP000051175; 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:UniProtKB-KW.
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; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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; PS51257; PROKAR_LIPOPROTEIN; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..112
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 737 AA; 79348 MW; 8C42B0493A51DF34 CRC64;
MTGTINRRSF IKMMGWGGVG TALGGCDVPT TVTLEEGKED VVSYLMPEEY VIPGVGVWYA
STCTQCAAAC GTQGRVREGR VLKMEGNPNS SVNSGKLCVM GQAGLQGHYN PDRIKEPMIR
KNGSLSLVGW DQALATINDK LNAADGARVA WFTGTISGHQ KVLLNALLES NGSSKHYVHE
VVGNKVLQAV SRDMLGDAMP KYRFDKAKMI LSFGADFLGS WMSSPVHFAG EYAKFRTNKP
RGLLVAIEPK MTLTGGNADL WIPARPGTEA AIALAIANEL INAHNKDAAI LPESVRNLIG
QHSAESVAKQ TAVAADRIKR LAQLLNERSP SLVLAGAPVE GQTNGYAATA AIMLLNHLLG
NIGQTIESPG AFAFAQLEAT TGGTADLIAF TQNAKDKNLD VAFFYGTNPV YSAPDALKFG
DALKNIGMKV AISQFMDETT AQADVILPAA SYLEDWGTHV AAYHSEQPAI SMQQPLMEKL
YETTRGFGDV LLALLQNKNK DKYGQYADYY AYLRHAFSAM PASYKENPAS EEHSWNAVLQ
KGVIKVQTTD ESLSTSIAEI DTPTIPASDS AYPLTLVPSV RLGLWDGRHA NLPWLQEAPD
QIAKVVWDSW AEIHPSTAKK LGIEQGSIIK VSSKHGEVTL KAVLLKGLHP DVVAIPMGQG
HTEYGRFAKG LGVNPLKILA PEQEQKTGEL AMYATNVKIT DTGKKDTVVK IGSTDTQMGR
KLVGTVPVEQ VRRTEGA
//
