ID A0YL95_LYNSP Unreviewed; 736 AA.
AC A0YL95;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:EAW38370.1};
GN ORFNames=L8106_10111 {ECO:0000313|EMBL:EAW38370.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38370.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW38370.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2006) 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}.
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:EAW38370.1}.
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DR EMBL; AAVU01000005; EAW38370.1; -; Genomic_DNA.
DR RefSeq; WP_009783251.1; NZ_AAVU01000005.1.
DR AlphaFoldDB; A0YL95; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000000737; 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 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; 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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 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 PIRSF; PIRSF000144; CbbBc; 2.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737}.
FT DOMAIN 2..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 81921 MW; 91E5687151CD576B CRC64;
MTEPTKTLCP YCGVGCGLDV LPPALPGKAT NRDKQGNPTW QVRGDRNHPS SQGKVCVKGA
TVSEALDKDR LTHPMMRESL DEPFRQVSWD EAFDRIVNQI QTVRVTQGPS GICMYGSGQF
QTEDYYIAQK LLKGCLGTNN FDANSRLCMS SAVSGYIQSF GTDGPPCCYD DLEQTDCAFL
IGTNTAECHP IIFNRLRVYH KKNKSVKMIV VDPRCTQTAE AADLHLAIKP GTDIDLLNGI
AHLLMKWGFF DSLFIDDCTK GFSDYAEVIR HYQPGLVARK CGIRLDDLET AARWWGESNR
VLSLWSMGMN QSSEGTAKVR TLINLHLMTG NIGKPGAGPF SLTGQPNAMG GREAGGLAHI
LPGYRVVKNP QHRAEVEEFW GLKPGSISPH PGLAAWDMIL GLEQNKVGLL WIAATNPAVS
MPDLERTKAA YRKSPFTVYQ DAYYPTETAA FAHVVLPAAQ WGEKTGTMTN SERMVTLCQA
FRSPLGVAKA DWEIFAEVGR RLGFAEQFDF ADSAAVRREF IQLTRNQPCE MSGITHEALS
QFGPIQWPCA ENSPDVAVHN KRLYTDFRFN TPDGRAKFGA YHSRGLAEPP DPNYPFVLTT
GRLYGQWHTQ TRTGRIEKIV KMHPEPFIEI HPRDAMKLSL QEGEIVEVRS RRGMARFPAK
ITKNITPGTV FVPMHWGSLW AELAEVNNLT HPESCPDSLQ PELKACAVQL IPVKEIRQTD
FESNNLVNQK LFAIRE
//
