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Database: UniProt
Entry: A0A150GIB5_GONPE
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ID   A0A150GIB5_GONPE        Unreviewed;       585 AA.
AC   A0A150GIB5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Ferredoxin--nitrite reductase, chloroplastic {ECO:0000256|ARBA:ARBA00040459};
DE            EC=1.7.7.1 {ECO:0000256|ARBA:ARBA00038893};
GN   ORFNames=GPECTOR_20g411 {ECO:0000313|EMBL:KXZ49557.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ49557.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) +
CC         nitrite + 6 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:18041,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036954};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000256|ARBA:ARBA00005096}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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:KXZ49557.1}.
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DR   EMBL; LSYV01000021; KXZ49557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GIB5; -.
DR   STRING; 33097.A0A150GIB5; -.
DR   OrthoDB; 5476448at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT   DOMAIN          125..188
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          200..357
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          382..446
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          459..561
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   REGION          30..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  64480 MW;  CBC33585DC2A0FD6 CRC64;
     MNSYQLRVQQ RSATSSRACR KSAVRVLATA APATTSNPAP PPHPLDGFKE HSGLKYLPEA
     ARTRALDKKA NKFEKVKVEK CGSRAWTDVF ELSHLLKEGN TKWEDMNLDD IDIRMKWAGL
     FHRGKRTPGK FMMRLKVPNG ELDAKQLRFL ASAIRPYGAD GCADITTRAN IQLRGVTLPD
     ADSIIKGLWE VGLTSFQSGM DSVRNLTGNP IAGVDPHELI DTRPLLRDME SMLFNDGKGR
     EEFANLPRKL NICISSTRDD FPHTHINDVG FEAVRRPDGE VVFNVVVGGY FSIKRNIMSI
     PLGCSVTQSQ LLPFTEALLR VFRDHGPRGD RQQTRLMWLV EAVGVDKFRE LLAEYMGGAE
     LAPPVHVHHE QPWERRDILG VHPQKQAGLN WVGACVPSGR MHAADFDEIA AVAEKYGDGT
     VRITCEENVI FVNVPDEKLP AMLAEPLFQR FKVNPGLLLR GLVACTGNQF CGFGLAETKA
     RAVKVVEALE EQLELPRAVR IHFTGCPNSC GQAQVGDIGL MGAPAKLDGK AVEGYKIFLG
     GKIGENPELA KEFAQGIPAL ESVLVPKLKE ILINEFGAKE KVVAA
//
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