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
//