ID A0A2G5B8I5_COERN Unreviewed; 1235 AA.
AC A0A2G5B8I5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=COEREDRAFT_44923 {ECO:0000313|EMBL:PIA15319.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA15319.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA15319.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA15319.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KZ303508; PIA15319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5B8I5; -.
DR STRING; 763665.A0A2G5B8I5; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000242474; 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 Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.90.480.20; -; 1.
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 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; 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 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); 1.
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:UP000242474}.
FT DOMAIN 498..646
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 1235 AA; 133953 MW; 372921C29335EA03 CRC64;
MPVAYAGAAN ASVVYVTFGA ELGTEAAGAA GVVQVSLFRP LCAAAFVEKV PATVKHLVAF
EQVTRQPTAW GPLLFDLAAV LHSSEWEARG GDKQPVLLDA VSAESPAAFA AAQLAEVTAH
AAGLKSPAHF NPAELVGIVG NSDKAQNETL EEQHGLSQEQ QQKRVEQIPY GHLLRDMFKE
RLNVANAAES RTIWGEGGQE SSNPEFGFGR LAAWEQERGR LVQAVTTALR DISVPLSKEL
QAGLSTWLSG RNDAAIATVA LAEQLGTQLE AEQEAHPAVE AVFQRRAWLT RQSNWLVGAD
EWAYDVGASG VHHVISSELN VNMLVLETAA YPFAPGTGRQ RKKDIGLYAM SYGTAYVASV
AVYASYTQVL QALAEADAFP GPAVVVAYLP HSAGVFSTSY SPIEVLRQSK QAVDSGAWPL
YRWDPTADAA RRFQLDSERL RRAVADFLRR ENALAAAGNA EPQLDVSEAT EARAAARLAR
KARGDVDALV GGLGGPGLLV LYASDNGNGE EAARRVARQG RRRGMAVRCV GMDAVDADEL
AFERTVVAVV STAGQGEVPT NGREFFKQLQ AASANFSETA FAVFGLGDSH YWPRAEDALF
YNKPARDLDR RLAELGAARI VDVGLGDDQD ADGWESGFGA FEQRLWGALN LDVVAGAGEE
DGPKRTDEEN KLISNFLRGT IAQAIADDST GAVDEWDGKL LKFHGTYMQD DRDLRAERMA
RGAEKAFSFM IRVRLPGGVA TPEQWLAMDR IADSHGNGSL KITTRQTFQL HGVLKRNLRD
TMRSINRALM DTIAACGDVN RNVVASANPL QAHLQPEVAA LAAELSSYLL PATSAYHEIW
LGDEQVAGSA EQTSGVEKQT APVADHEPLY GPTYLPRKFK IAIAIPPEND VDVVAYDLGL
IAILDDSQRT IVGYNVMVGG GMGMTHNNRA TYPRLASCLG FVTKDAVLAV AKAVLLVQRD
HGDRVNRKHA RLKYTVDDHG LPWWRAQVEV RMGARLEEPR PYEFTRNGDR YGWVATTPGL
NNFTMFVQNG RVVNLPGRPL KDALAAVARK HTGLFRLTCN GHLIVADVRD EDVPAMSALL
ASHGLDNLDY SALRLHSMAC VALPTCGLAM AESERYLPRL IDLLDAIIDS AGLRNDAIVI
RMTGCPNGCA RPYNAEIAFV GKAPGAYNLY LGGSHSGERL NKLYRETVTE DQILELLTPI
IKQYALERLP AEHFGDFVIR KGIVKETREG KDFHD
//
