ID Q3AVP6_SYNS9 Unreviewed; 743 AA.
AC Q3AVP6;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Assimilatory nitrate reductase (Ferredoxin) {ECO:0000313|EMBL:ABB27230.1};
DE EC=1.7.7.2 {ECO:0000313|EMBL:ABB27230.1};
GN OrderedLocusNames=Syncc9902_2272 {ECO:0000313|EMBL:ABB27230.1};
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB27230.1, ECO:0000313|Proteomes:UP000002712};
RN [1] {ECO:0000313|Proteomes:UP000002712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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; CP000097; ABB27230.1; -; Genomic_DNA.
DR RefSeq; WP_011361006.1; NC_007513.1.
DR AlphaFoldDB; Q3AVP6; -.
DR STRING; 316279.Syncc9902_2272; -.
DR KEGG; sye:Syncc9902_2272; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_3; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002712; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047889; F:ferredoxin-nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; 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 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.
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 ECO:0000313|EMBL:ABB27230.1}.
FT DOMAIN 5..73
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 30..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82274 MW; 118FBBFBDDB91C78 CRC64;
MTQSPRSVRS QCPYCGVGCG LELLPPAEKG RPVRRDAEGN PMWTARGDRQ HPSSLGQVCI
KGATVGETLA SGRLRQPLFR SNFSDDFEPI GWDDALERIT KQMTCSLERR GHANGIAMYG
SGQFHTEDYY VAQKLMKGAL GTNNFDANSR LCMSSAVAGY TRSLGSDGPP CCYDDLDHCS
VAFLIGTNTA ECHPVLFQRL LKRKKRNPGS VTIVVVDPRR TDTAKAADIH LPIAPGSDLA
LLHGIAHLIL RENGQDPAFI DDHTENYEAF FDVVARWTPR RVARFCNLPE KRLREVAQLF
HRREDVLSLW SMGVNQRQEG TAVVCGLINL HLLTGQIGKE GAGPFSLTGQ PNAMGGREAG
GLSHLLPGYR FVANGQHRQD VEQAWDFPAG SIAATPGLAA WQQIEAMERG ELDLWWVAAT
NPLVSMPDLD RVKAAMSKCP LVVVSEAYAD SETSHYAHLL LPAAQWSEKA GAMTNSERRI
TYCPAYRRRF GESRPDWEVF AEVGQRLGFE KQFHFNSAAD VYAEFAELTR GRLCDMSGLS
HALLSEEGPQ QWPYPSESTT PCESKRLYTD HHFATPSGRA RFSIDQPLGL AEPPCDTFPL
VLTVGRYLGQ WHTMTRTGKV ERLHTMHPEP LLEIHPGDAQ ELKVVNGELA AISSRRGHIT
ATVKVTDRIR RGSVFLPMHW GFTQENACEA NTLMHDQACP ISKQPELKAC AVIVAPAVSM
VKPIEQEKGR LEALRRLLTP TLR
//
