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Database: UniProt
Entry: A0A0B7MUU4_9FUNG
LinkDB: A0A0B7MUU4_9FUNG
Original site: A0A0B7MUU4_9FUNG 
ID   A0A0B7MUU4_9FUNG        Unreviewed;      1624 AA.
AC   A0A0B7MUU4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN   Name=PARPA_00117.1 scaffold 340 {ECO:0000313|EMBL:CEP06863.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP06863.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP06863.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP06863.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; LN718797; CEP06863.1; -; Genomic_DNA.
DR   STRING; 35722.A0A0B7MUU4; -.
DR   OrthoDB; 5474937at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
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:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; 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   HAMAP; MF_01540; CysI; 1.
DR   InterPro; IPR011786; CysI.
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; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR02041; CysI; 1.
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; PF17147; PFOR_II; 1.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT   DOMAIN          897..1049
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   1624 AA;  178220 MW;  09595CD9D01BFC5C CRC64;
     MQHKTYLWNG ESASIQASQL LSQHIYTYRN IECSNSSSTN IWGKSSGHTV YSQQDITSRL
     QHGVHSAALV SSDSLISAIP QLYKLASEKS GVVLHVSAKH GDSSSFADFS NVMAVRQSGL
     TFLSSSTVQE AHDLAVIAHM VAIKTSTPVL HFFDSKRIAQ EFASIDLVTI DILNQLISAE
     DIEHYQQQQQ QQQQQQQQQS AYLQYKQQQA EEKDGKDVDV YAVVQEAMAQ FAALTGRHYA
     PLEFIGHPEA EDVIIAMGAG ATVVEKTVNA LGKDAKLGLL KVRLYRPWSD TDLLASLPGA
     SIKRVAVLEP SHDVTCTWNP LFLDIAAAYQ TAEDNDVEII SGQYGVKDQD FSPAQVQAVF
     SELGKADFQR KFEVAALKTA AADQLVKVVP EETEQFLVVG DETLALKYAQ AAVSAGKYAQ
     VYTVEEVSHI RVSGSAGSFL PSLVSEAKAV VLQNASIDAA DAVKALIPGG VIVVSSAAVS
     EGLDVALAET TKRSIGVAHV KIVELTNVED LVSAGGLHSV LSKAEAVATP SGWDQLTGAA
     TATATLKTAD KAALAVETPY LKMLDQVFQD RLEIANAVNS ASVWSRDEQK QSASAPEFGY
     GKILSKIQKR ARFIDAVETL VKDNKVSEEA YKTLSQWLLV VKSHKSDAKA INKAAKAVVS
     AIANVSAAEY VAQNKDLLFQ KSNWLIGSDS WAYDLGQSGV HHVIAQGENV NMLIVDTLPY
     SSSDLAREQR KKDIGLYAMN FGSAYVASVA VYSSYTGVLH ALMEADAYQG PSIVLAYLPQ
     EPTGANAASN PVFTMKETKV SVDNGAWPLY RWNPSLEAQG KEAFSLDSQR IKKDLEKFLE
     RENHFSQIVA QHPDISQLLV SSLENDVEKR HSELKRKARQ DFAKLLSGMG AANGPPLLVL
     FGSDNGNAEG VAKKIANRAK SRGLQVKLMA MDDYEDVQEL ANETNVVFIV STAGQGELPS
     NGRELWKALN GLIVGDADFS QLNFAVFGMG DSHYWPREED AMFYNRPGKL IDAKLETLGA
     NRLVEIGLGD DQDADGFETA LAVWQPEFWR SLGVKDVGAE DDEPKLTDDQ MKINSNFLRG
     TIAQDLLDES TGAISEINGK LLKFHGSYGQ DDRDIREERK KMGLEKAFSF MIRVRMPGGV
     STPEQWLVMD ELADTYANGA IKLTTRQAFQ LHGILKKNLR STIRGINHAL LSTLAACGDV
     NRNIMITPVT EIPEVHAQVQ EFGMVLMEHL APKTTAYHEI WLADEQVAGN AVQDFEPIYG
     PTYLPRKFKI VIAVPPNNDV DIFAHDLGYI AIVDDNKKVI GYNVTIGGGM GMTHGNKKTY
     PRPANVVGYI PAELAVACGE AVMTTQRDYG DRTNRKHARF KYTIDTHGLD FIKNEIETRM
     GVKFEQARSY VFADNADRYG WTKGVDDKWH FCMFIENGKI KDWPDFQPKT GLKELAKWHK
     GEFRLSPNQH LVIANVPEAD LEKTKALLAK YKMDNLSFTG LRLNAMACVA LPTCGLAMAE
     SERYLPTLVG HLENAIEAAG LKDDAITIRM TGCPNGCARP YLAEIAFVGK APNTYNVYLG
     GGHQGQRLNK LYKESLREQE ILEEINPIIK RYASERLSGE PFGDFVIRAG YVKETITGTD
     FHEL
//
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