ID A0A2S6CW53_9CYAN Unreviewed; 716 AA.
AC A0A2S6CW53;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Nitrate reductase catalytic subunit {ECO:0000313|EMBL:PPJ63820.1};
GN ORFNames=CUN59_08065 {ECO:0000313|EMBL:PPJ63820.1};
OS Cuspidothrix issatschenkoi CHARLIE-1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Cuspidothrix.
OX NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ63820.1, ECO:0000313|Proteomes:UP000239589};
RN [1] {ECO:0000313|EMBL:PPJ63820.1, ECO:0000313|Proteomes:UP000239589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ63820.1,
RC ECO:0000313|Proteomes:UP000239589};
RA Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT cyanobacterium.";
RL Submitted (FEB-2018) 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:PPJ63820.1}.
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DR EMBL; PGEM01000052; PPJ63820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CW53; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000239589; 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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000239589}.
FT DOMAIN 1..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 716 AA; 80038 MW; 010A5D092A3A23F8 CRC64;
MESIKTLCPY CGVGCGLEIT PLAQKEHQPW RVKGDRSHPS SQGMVCVKGA TITESINKNR
LHYPMFRKSL NEDFQRISWD EAFNLITQHI QETLVNHGAE SICMYGSGQF QTEDYYIAQK
LLKGCLGTNN FDANSRLCMS SAVSGYIQSF GSDGPPCCYD DLELTDCAFL IGTNTAECHP
ILFNRLVKYH KKNHHVKMVV VDPRRTPTAE AADLHLAIRP GTDIDLLNGI AHLLMKWNYI
DTTFIDDCTS NFPAYVEVIR YYSPDVVARQ CGISIEDLEI AAKYWGQAKS VLSLWSMGVN
QSSEGTAKVR TIINLHLMTG QVGKPGTGPF SLTGQPNAMG GREAGGLAHL LPGYRLVKND
QHRAEIEDFW KLERGKISPI PGLTAWDMIT GLECGNVNLL WVAATNPAVS MPDLERTKKA
LLKSPFTIYQ DAYYPTETAA YAHLLLPAAQ WGEKTGIMTN SERRVTLCQA FHQPPREAKA
DWEIFAEVGK RLGFNNKFNF NNSAEVYQEF VQLSHQRPCD MSGLSHEFLA TNGPTHWPYS
QGSNSETKRL YTNLRFNTQD GRAKFGAYHS KGLAEPPDPN YPFILTTGRL YGHWHTQTRT
GRIDKIRTMH PEPLMEIHPR DAAQLGIVDN QVVEVRSRRG VAKFPAKITK AISPGTVFVP
MHWGKLWAEN SEANALTHSE SCPDSLQPEL KACAVQLLPI SLKTTAKNYQ VLSSQR
//
