ID A0A1F5LRX3_9EURO Unreviewed; 1083 AA.
AC A0A1F5LRX3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN ORFNames=PENARI_c003G03891 {ECO:0000313|EMBL:OGE55895.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE55895.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE55895.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE55895.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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}.
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:OGE55895.1}.
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DR EMBL; LXJU01000003; OGE55895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LRX3; -.
DR STRING; 1835702.A0A1F5LRX3; -.
DR OrthoDB; 275583at2759; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide 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-UniPathway.
DR CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 3.30.390.30; -; 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; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
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 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 PRINTS; PR00469; PNDRDTASEII.
DR PRINTS; PR00397; SIROHAEM.
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; PS00365; NIR_SIR; 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:UP000177622}.
FT DOMAIN 915..1019
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120142 MW; 9A575C0B08EFAEE3 CRC64;
MPVLDGLRHG EPVDGSPSPA NNVHREKIVV VGLGMVAISF IEKVIKQDTD RKYDIVVIGE
ESHVAYNRVG LSTFFEHRKI EDLYLNPKEW YGSFKERAFD HHLNTRVTEI NPTNKTVQTS
TGDIISYDIL VLATGSDATL PTRTPGHDAN GVFVYRTISD LERLIDFASK HKGKTAVTVG
GGLLGLEAAK AMTDLEDFGN VKLIDRNRWV LARQLDGDAG SLVTRKIREL GLDVLHEKRV
KVVHTDEGNN VVGITFEDGE RIDCCCICFA IGVQPRDELG RGIGIQCGER GGFVIDENLQ
TSVPGIYAVG ECASWENQTF GIIAPGIEMA DVLAFNLTNP RKAQKSFTRP DLSTKLKLLG
VDVASFGDFF ADRDGPKFLP GRRPSAVPGF EEPLRDEPVK ALTYKDPFAG VYKKYLFTMD
GKFLLGGMMI GDTKDYLKLN QMVKLQKELE VPPSQFILGA QSGGEENADD LDDSTQICSC
HNVTKGDVVD NVKNGTCTSI AEVKSCTKAG TGCGGCMPLV QSIFNKTMLD MGQEISNNLC
SHIPYSRADL YNIVAIKQLK TFVDVMKTAG KNPDSLGCEL CKPAIGSILS SLFNPHVMDK
GYNDLQDTND KFLANIQRNG TFSVVPRVPG GEITADKLIA IGSVAKKYGL YCKITGAQRI
DMFGAKKQDL LNIWTELVDA GMESGHAYAK ALRAIKSCVG TTWCRFGVGD SVGMAIRLEE
RYKSIRAPHK FKGAVSGCVR ECAEAQNKDF GLIATEKGFN IFVGGNGGAK PRHAELLVTD
VPPEMVMPII DRYLIFYIRT ADKLQRTARW IENLPGGIHY LKEVIVEDKL GICADMERQM
HELVDSYFCE WTETVKDPKR RKVFQQFANT DDTVETVEVV QERSQQRPTY WPKDSTEQQD
FKGHQWSSVS WQPVVRADHF SDEPPQVSSA NVKRGDTQLA VFKIKGKYYA TQQMCPHKRA
FVLSDGLVGD DDAGKYWVSC PYHKRNFDLN GEQAGRCSND ESMNIATFPV EERDDGWVYM
KLPPIEELDG VLGTEKWKIR KDESEDPFHK VDKKFKGMKG KKASSGNILS RAPAVQPAKT
IDW
//
