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Database: UniProt
Entry: A0A0S9RAS9_9ACTN
LinkDB: A0A0S9RAS9_9ACTN
Original site: A0A0S9RAS9_9ACTN 
ID   A0A0S9RAS9_9ACTN        Unreviewed;       714 AA.
AC   A0A0S9RAS9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KQP79178.1};
GN   ORFNames=ASF37_10965 {ECO:0000313|EMBL:KQP79178.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP79178.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KQP79178.1}.
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DR   EMBL; LMNK01000002; KQP79178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9RAS9; -.
DR   Proteomes; UP000051640; 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:InterPro.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-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   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 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.
PE   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000051640}.
FT   DOMAIN          1..51
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|SMART:SM00926"
SQ   SEQUENCE   714 AA;  75860 MW;  B73A161892999C25 CRC64;
     MTDTDTHCPY CALQCAQRLG GHPLAAEPRD FPTNRGGMCQ KGWTSAELLR TPDRLVEPLR
     RTPRGLRPVS WEEALDDIAD RSLSLAEQHG PDALAVFGGG GLTNEKAYQL GKFARLALRT
     RMVDYNGRFC MSSAAAAANR SLGVDRGLPF PLTDLRDADA VLLLGSNLAD TMPPAVQHLA
     GAREQGGLVV VDPRRSATAR LCDDGAGTHL QLVPGTDLAL LLGLLHVVLG EGLADTAYLH
     ERVDGVEEVR RSVASWWPER VASVTGVPEP QLRAVARRLA DASPHRGGRG AFVLTGRGAE
     QHTDGTATVS AAISLALALG LPGAERGGYG ALTGQGNGQG GREHGQKADQ LPGYRSIEDP
     AARAHVAGVW GVDPDAIPRS GVPAVELLAG LGTADGPRGL FVHGSNLVVS APRAGAVRER
     LASLDLLVVC DVVPSETALM ADYVLPVTQW AEEEGTMTSL EGRVLRRRRA VTAPPQVRDE
     LWIWAELARR LDAPGTWSTE SREVFDELAR ASAGGRADYA GIAHDRLDRG EALYWPCPDP
     THPGTPRLFT ERFPTASGRA TMVPVSSDGP DDAVREDAPI HLVTGRLLQH YQSGAQTRRV
     PALRQAAGEA HVEMHPALAA RLGVDAAELV RVTSTRGSMV APARLTRDIR PDTVFAPFHF
     GGDGLVNAVT NDATDPVSGM PEFKVCAVTV ERVEPGAGVR RPTGAPTTLL EVES
//
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