ID A0A1N6Z1D8_9ACTN Unreviewed; 812 AA.
AC A0A1N6Z1D8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Molydopterin dinucleotide binding domain-containing protein {ECO:0000313|EMBL:SIR20620.1};
GN ORFNames=SAMN05444858_107129 {ECO:0000313|EMBL:SIR20620.1};
OS Micromonospora avicenniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIR20620.1, ECO:0000313|Proteomes:UP000186004};
RN [1] {ECO:0000313|EMBL:SIR20620.1, ECO:0000313|Proteomes:UP000186004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45758 {ECO:0000313|EMBL:SIR20620.1,
RC ECO:0000313|Proteomes:UP000186004};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTNF01000007; SIR20620.1; -; Genomic_DNA.
DR RefSeq; WP_076470694.1; NZ_FTNF01000007.1.
DR AlphaFoldDB; A0A1N6Z1D8; -.
DR STRING; 1198245.SAMN05444858_107129; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000186004; 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 CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02754; MopB_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; 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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186004}.
FT DOMAIN 39..95
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 783..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 88418 MW; 14A3231236904DB4 CRC64;
MVDRIADPWG PRTPYGSGQE WPVRVDTFLD GDLNAEDVDR WVQSASILHS NGDALDIAVR
DGRIVGVRGR AVDRVNRGRV DPKDLYGWQA NNSPDRLTRP LVREGGRLVE TDWDTAMGRI
VARSKELLEG PGGWGHFGFY TSGQLFLEEY YTLGVIGKAG LGTPHMDGNT RLCTATAAAA
LKATFGADGQ PGSYADVDHC DAIAIWGHNV AETQTVLWMR MLDRRRGPNP PALLAVDPRS
TAVTREADLH LPIRNGTNMA LLNGLLREVI QHGWYDEAYV DAHTLGFDEL CRTVDGYPPE
LVADICDIPA ADVRRAAELL GGSQRLLSTV LQGFYQSNQA TAASCQVNNL HLIRGMIGRP
GAGIYQMNGQ PTAQNTRETG ADGDLPGLRN WDNPEHIAEL ARLWNVEPEV IPHWAPPTHA
MQIFRYAEQG SVKLLWISAT NPAVSLPDLS RIRRILRQPE LFVVVQDLFL TETAELADVV
LPAATWGEKT GTFTNVDRTV HLSEKAVDPP GEARADLDIF LDYARRMDFR DLDGRPLVKW
TTPEEAFEAW QECSRGRPCD YTGLTYDRLR GGSGIQWPCN DANPDGTERL YADAVFPTDP
AVCETYGQDL DTGAEFLADE YRAKQPGGRA FLHAVEYRPS PEVPDEEHPM LLTTGRTVYQ
FHTRTKTGRA PQLNSAAPDV WVELNPADAG RLGIAEGDLV GIASPRGAVQ ARARLSGIRP
GVVFLPFHYG WFDQDPADRT PRAANELTIT AWDPVSKQPL FKVAAVAVTR LADGGGVPAP
APTVGGSAPA VAGVPATVGG PAAEANSRAG GE
//
