ID A0A0Q9SGX9_9MICO Unreviewed; 732 AA.
AC A0A0Q9SGX9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KRF22964.1};
GN ORFNames=ASG91_16550 {ECO:0000313|EMBL:KRF22964.1};
OS Phycicoccus sp. Soil802.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF22964.1, ECO:0000313|Proteomes:UP000050906};
RN [1] {ECO:0000313|EMBL:KRF22964.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF22964.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF22964.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF22964.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Schulze-Lefert P.;
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:KRF22964.1}.
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DR EMBL; LMSS01000006; KRF22964.1; -; Genomic_DNA.
DR RefSeq; WP_056923700.1; NZ_LMSS01000006.1.
DR AlphaFoldDB; A0A0Q9SGX9; -.
DR Proteomes; UP000050906; 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; 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.
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}.
FT DOMAIN 11..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 732 AA; 76170 MW; A544689B8667BE6E CRC64;
MTTTSTSTVR ADSVATHCPY CALQCAQTLT ANPGVDGANG VIVEGRAFPT NRGGLCQKGW
TSAEVLTSPD RLTSPLVRGV DGELAPSSWE DALDLVADRL LAIRRDSGPD AVAVFGGGGL
TNEKAYQLGK FARVALGTAN IDYNGRFCMS SAAAAANRSL GVDRGLPFPL TDLASADAVL
LLGSNLAETM PPSVAHLAGV RGRGGLVVVD PRRSATADLA ADGQGLHLQP VPGTDLVVLL
ALQHVLLTDG LVDADYLERR TNGLEDVKRR SALWWPERAE QVCGVPADLL RDTARLLAAA
SPSRGGTGAF VLTGRGVEQS RQGTATVSAA ITLSLLLGLP GRVGSGYGAV TGQGNGQGGR
EHGQKADQLP GYRMIDDPAA RAHVAAVWGV SPESLPGKGM PAVELLASLG TADGPRALLV
HGSNVLVSAP NVHRVADRLA ALDLLVVCDF VPSETALLAD VVLPVTQWAE EEGTMTSLEG
RVIRRRKAVE PPAGARSELW VWAQLAARLG AAGTWDTEPS LVFDELARAS RGGRADYSGL
SHARLDGDEA LHWPCPATGD GEPNHPGTPR LFAESFPTPD GRARMVAVDH LGPADDLRPD
APLYLVTGRV LQHYQSGAQT RRVPALAGAV PGAFAEVHPL LAARIGIADG ERVRLTTARG
SLAVPARVTD SIRPDTVFVP FHWAGTGSVN RLTTDATDPV SGMPEFKVCA VDVTAARVQP
AGSARPTAGV PA
//