ID   A0A1C4DLJ6_9ENTR        Unreviewed;       812 AA.
AC   A0A1C4DLJ6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase subunit A {ECO:0000313|EMBL:SCC32125.1};
GN   ORFNames=GA0061070_101712 {ECO:0000313|EMBL:SCC32125.1};
OS   Kosakonia oryziphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kosakonia.
OX   NCBI_TaxID=1005667 {ECO:0000313|EMBL:SCC32125.1, ECO:0000313|Proteomes:UP000198515};
RN   [1] {ECO:0000313|Proteomes:UP000198515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=REICA_142 {ECO:0000313|Proteomes:UP000198515};
RA   Varghese N., Submissions Spin;
RL   Submitted (AUG-2016) 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FMBC01000017; SCC32125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4DLJ6; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000198515; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR   CDD; cd02770; MopB_DmsA-EC; 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   InterPro; IPR011888; Anaer_DMSO_reductase.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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          54..116
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   812 AA;  90132 MW;  84235CC60A192FAF CRC64;
     MNMKMSDELL DAEVSRRGFM KTTALGGLAV ASSTFALPFT RLASAADAIT PVQENVVWSA
     CTVNCGSRCP LRMHVVDGEI KYVETDNTGD DNYDGLHQVR ACLRGRSMRR RVYNPDRLKY
     PMKRVGKRGE GKFERISWQE AFDTITNNMQ RLIKEYGNES IYLNYGTGTL GGTLTRSWPP
     GKTLIARLMN CCGGYLNQYG DYSSAQIAAG LNYTYGGWAD GNSPSDIENS QLVVMFGNNP
     GETRMSGGGV TYYIEQARQK SNARMIIIDP RYTDTGAGRE DEWIPIRPGT DAALVSALAW
     VMITENLVDQ PFLDKYCVGY DEKTLPADAP ANGHYKAYIL GQGNDGIAKT PEWASVITGI
     PQARIITLAR EIASTKPAFI SQGWGPQRHA NGELVSRAIA MLAILTGNVG LNGGNSGARE
     GSYELPFVRM PTLENPVQTS ISMFLWTDAI ERGPEMTATR DGVRGKDKLD VPIKMIWNYA
     GNCLINQHSQ INRTHDILQD DKKCELIVVI DCHMTSSAKY ADILLPDCTA SEQMDFALDA
     SCGNMSYVIF ADQAIKPRFE CKTLYEMTSE LAKRMGVEQQ FTEGRSQEEW MRYLYEQSRQ
     AIPDMPTFDA LRKQGMFKQR DPAGHHVAYK TFRDDPQKNP LTTPSGKIEI YSAQLAAIAA
     SWELDKEDVI DPLPVYSAGF ENYNAPLSKT YPLQLTGFHY KARTHSTYGN VDVLNAACRQ
     EMWINPIDAQ LRGISNGDRV RIFNDRGEVQ IEAKVTPRMI PGVVALGEGA WYNPDARRVD
     QAGSINVLTT QRPSPLAKGN PSHTNLVQVE KA
//