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Database: UniProt
Entry: A0A1V6Z3W9_PENNA
LinkDB: A0A1V6Z3W9_PENNA
Original site: A0A1V6Z3W9_PENNA 
ID   A0A1V6Z3W9_PENNA        Unreviewed;      1526 AA.
AC   A0A1V6Z3W9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN   ORFNames=PENNAL_c0004G07955 {ECO:0000313|EMBL:OQE94375.1},
GN   PNAL_LOCUS415 {ECO:0000313|EMBL:CAG7948352.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE94375.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|EMBL:OQE94375.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE94375.1};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
RN   [3] {ECO:0000313|EMBL:CAG7948352.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Branca A.L. A.;
RL   Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:OQE94375.1}.
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DR   EMBL; CAJVNV010000011; CAG7948352.1; -; Genomic_DNA.
DR   EMBL; MOOB01000004; OQE94375.1; -; Genomic_DNA.
DR   STRING; 60175.A0A1V6Z3W9; -.
DR   OMA; YGSYTQV; -.
DR   OrthoDB; 5474937at2759; -.
DR   Proteomes; UP000191691; Unassembled WGS sequence.
DR   Proteomes; UP001153461; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   Pfam; PF01855; POR_N; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT   DOMAIN          782..931
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   REGION          213..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1526 AA;  168253 MW;  771AE469478909C7 CRC64;
     MVSISSAAEA VARIAYLTSD TVLSVQPSLQ NDSLFSKSLK ALKSNKTSNL SSKVTEVQAV
     RYNEDPLLSV FTPLQNGETT SIVTSSSVLI TAVPHLYRLA NSPVVIHVAL EPSPFPDYSV
     ISSIRQSGFT FLHSETVQEA QDIAITAHAL ARKSGKGVIH FFDPSNSAKD PSIPEEDIEV
     VKKVLSVGGN SAISAGTQTL YADSGRVATV TAETVGTSPS GQSESTNLTV PSQPQTPFNA
     SVDNSSVGSS RRDSSAGSET PSSTATTVDS ATIRPVNAAD IFDWTAQIWN TLFEEVGRRY
     NAIEYTGVAD AKSAIFVFGS TGVFVDALAN AGANPELENI GLITARLYRP WVGGQISNSI
     PSSVEKIAVL EQVRKTTRWG PSFMDLLSSL TPSGARAQPP QIVGYRLGYI EPSTAVQALR
     GVLQNLNSAS PIQNLDIGSS QVPVVQHALE QPRIENAYLK ILDQLFGERL HIANQLGSNN
     AGISSTIAAS PEFGFGSLLA RQEHRQRFIR EVEEATRSNG FATDVPKTWL SRWALNVKEA
     AKANKLAPDV ISRLSNDGSA ISRQLLQSKQ LFYEESDWLV GSDAWAYDLG NSGVHHVLAS
     GANVNMLIID SQPYSERTAS DANRRKKDIG LYAMNRGTAY VASVAVYSSY TQVLQAMSEA
     QQFKGPSVVV AYLPYNQEND SALTVLQETK KAIDLGYWPL YRWNPDNEEK GEPKFQLDSE
     RIKRDLEEFL RRDNQLTQLM NRQPKYAPVL SESYGTEVRA LQKRNAKDSY EKLLDGLFGA
     PLTILFASDG GNAQNIAKRL GNRGRARGLK TMVIAMDEFP LEDLPTEENV VFITSTAGQG
     EFPVNGRSLW EHVKNTGDLD LSTINYSVFG LGDSHYWPRK EDKIYYNKPA KDLDDRVAFL
     GGRKLTDIGL GDDQDPDAYQ TGYSEWEPRL WKSLGVDKVE GLPEEPAPIT NEDIKINSNF
     LRGTIAEALL DESTGAIPAS DQQLTKFHGT YMQDDRDLRD ERKAQGLEPA YSFMIRCRLA
     GGVATPKQWL QMDAISSSHG NETMKLTTRQ TFQFHGVIKR NLRGAMRAIN NSMMDTLAAC
     GDVNRNVMCS SLPELSSVHR ETWAISSKIS EHLLPSTTAY HEIWLKDDND KKVQVAGDAV
     VDHEPLYGPT YLPRKFKITI AIPPHNDTDV YAHDIGLIAI KGADGNLEGF NVLAGGGMGS
     THNNTKTYPQ TGRMFGYIPK DMVHIACEKI MLVQRDNGDR KNRKHARMKY TIDDMGVDAF
     RSEVENRLPD GLKFGEPRPF EFKSNVDTFG WLKDDTGLNH FTFFIENGRI EDTADFKMRT
     GLRELAEMGK GEFRLTGNQH LMISRITDED LPAIKEHMAK YKLDNTAFSG LRLSSSACVA
     FPTCGLAMAE SERYLPVLIS KLESTLEECG LARDSIVMRM TGCPNGCARP WLAEVAFVGK
     AFGAYNMYLG GGYHGQRLNK RYRSSIKEDE ILEIMKGLLK RYSLERDTDG ETPERFGDWC
     IRAGVIKATT DGKDFHDGVA EDEEEE
//
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