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Database: UniProt
Entry: F0X9I4_GROCL
LinkDB: F0X9I4_GROCL
Original site: F0X9I4_GROCL 
ID   F0X9I4_GROCL            Unreviewed;      1103 AA.
AC   F0X9I4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:EFX05412.1};
GN   ORFNames=CMQ_3481 {ECO:0000313|EMBL:EFX05412.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX05412.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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}.
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DR   EMBL; GL629735; EFX05412.1; -; Genomic_DNA.
DR   RefSeq; XP_014174894.1; XM_014319419.1.
DR   AlphaFoldDB; F0X9I4; -.
DR   STRING; 655863.F0X9I4; -.
DR   GeneID; 25976586; -.
DR   eggNOG; KOG1336; Eukaryota.
DR   HOGENOM; CLU_003291_0_0_1; -.
DR   InParanoid; F0X9I4; -.
DR   OrthoDB; 275583at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR012748; Rieske-like_NirD.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   NCBIfam; TIGR02378; nirD_assim_sml; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13806; Rieske_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT   DOMAIN          926..1012
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          837..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  119416 MW;  6719D2A0C83BCC54 CRC64;
     MATNTRKKVV VVGLGMVGIS FIEKLLKLDA RARDYDIVVF GEEEHLAYNR VGLTTYFGHR
     QAEKLYLNRR DWYESIADGA LRYHTSKRVA AIDTESKTVM CEDGSAEGYD ILVLATGSDA
     VLPRQTPGHD AQGVFVYRNI ADLEKLIRYE SSGVGAVVGG GLLGLEAAKA MIDLGRFDKV
     VVIERNSWVL SRQLDDEGGG MVVESVQKLG VEVLLRKRVK IVLTEGIEGE GGESKRVIGV
     QFEDGEKLAL STVCFAIGVR PRDELARAAG IECAERSSGG VVVGDDLQTS AADVYAVGEC
     ASWHGQTFGL IGPGVEMADV LAFNLTQAKL HKVRSFRRPD LSTRLKLLGV EVASFGDFFA
     DRDGPMGLPA KAKRGKAGGE ARAAAGTAAV KALTYKDPFR GIYKKYIFTA DGRFLLGGMM
     IGDTSDYVRL VAMVTKQKEL DRAPGELIVG ARASDEAGAN ELDDETQICS CHNVSKGAVV
     AAVRDGGCTS LGAVKACTKA GTGCGGCVPL VTSIFRTAMA ALGNEVSQDV CAHFRHSRAD
     LYHIVAVRGL KTLAEVMAAA GVRADSVGCE VCRPVVGSIL ASQWNGHVMR GPTQALQDTN
     DRWLGNMQRD GTFSVVPRVA AGEITPARLV VLGEVARDFG LYAKITGGQR IDLFGARRPD
     LPAIWQRLVD AGMESGHAYA KSLRTVKSCV GTTWCRYGVG DAVGLAVRLE ERFGLIATEK
     GFNIYVGGNG GATPRHAELL ARDVAPADVV PILDRYLALY IRTADRLQRT ARWIEALPGG
     VAYLRDVIVH DRLGLAAELE AQMAELVGSF FDEWAEALRD PALLARFRQF ANTEERLAGE
     AERETERQQE RPVFEKRGME VEVEVEVDGG RVEKDPKKDP RKDPRKDPRK GLKDPEKDRD
     FAALTNSWST LAWQPVLDVA TFDRQTGTAS TSSTTDVAAT TVKLGDTQLA LFRVRGHYYA
     TQQMCPHKRA FVLSDGLIGD DPTDRQQPWV SCPLHKRNFD LGSGACRSDP ASGLSLATFA
     VRVEPEPKPE QEKQTIAICL PPPAELDAAL GTARWRLRAG EAGPPQLAEL DRRLQPSLVG
     RRASKTIDRR PAAPITAGGG LDW
//
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