ID   A0A1H0EE85_9ACTN        Unreviewed;       826 AA.
AC   A0A1H0EE85;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Molydopterin dinucleotide binding domain-containing protein {ECO:0000313|EMBL:SDN80797.1};
GN   ORFNames=SAMN05428965_1708 {ECO:0000313|EMBL:SDN80797.1};
OS   Geodermatophilus sp. DSM 45219.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDN80797.1, ECO:0000313|Proteomes:UP000198730};
RN   [1] {ECO:0000313|EMBL:SDN80797.1, ECO:0000313|Proteomes:UP000198730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45219 {ECO:0000313|EMBL:SDN80797.1,
RC   ECO:0000313|Proteomes:UP000198730};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747}.
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DR   EMBL; FNIQ01000002; SDN80797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0EE85; -.
DR   STRING; 1881103.SAMN05428965_1708; -.
DR   Proteomes; UP000198730; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 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   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 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; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
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   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          49..105
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          784..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   826 AA;  90361 MW;  40A169B5A2188806 CRC64;
     MGRGYATVMP RTDRIAEPWG TRTPYGPGGT WPTRVDQYLA DGLTEDDVDR WVQSATILHS
     NGDGLDIAVK DDRIVGVRGR AVDRVNHGRL GPKDLFGWQA NNSPDRLTRP LIRRRGKLVE
     TDWDTAMDAV AGRCRQLLDE RGPSAISFYT SGQLFLEEYY TLGLIAHGGI GTNHVDGNTR
     LCTATAAAAL KETFACDGQP GSYTDVDHAD VIALYGHNMA ETQTVLWTRV LDRLAGPNPP
     KIICVDPRET PVARAATVHL APRPGTNVML VNALLHEIIG NGWIDREYVA AHTVGFAELE
     EQVAAYPPEV AAEVCDVPAE QIREAARILG HAERLLSTVL QGFYQSHQAS AAAVSVNNVN
     VVRGMLGKPG CGILQMNGQP TAQNTREAGA DGDLPAFRNW SNDAHVQDLA RIWNVDPMQI
     PHHSPPTHVM QQLRYMEEGS IRFLYVTATN PAVSLPELRR IRSILAQERL FLVVQDIFLS
     ETAQLADVVL PAATWGEKTG TFTNVDRTVH LSEKAVEPPG EARADLDILI DFAHRLGLRD
     EDGAPLVKWS DAEGAFEGWK ECSRGRPCDY SGMTYDKLRG GSGIQWPCTD EHPEGTERIY
     VDGQFWAQPE YCESYGRDMV TGAPVEETEY KALNPTGKAV LKAAEYLPPH ELPSREYPFQ
     LITGRTLYHF HTRTKTGRAP QLQAAAPDVW VEMSAGDAAD RGLAEGDLLE VSTPRGRVRA
     RLRVSGIRPG VLFLPFHYGY WDTEGSRPRR KGGGRAANEL TLTDWDPVSK QPIFKTAAAR
     VERVARGRGA PAPAPTTTGS APVAGSVPPT TGGDDARAEE RVGGRS
//