ID   H8WZW7_CANO9            Unreviewed;      1443 AA.
AC   H8WZW7;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Ecm17 enzyme of sulfur amino acid biosynthesis {ECO:0000313|EMBL:CCG22312.1};
GN   ORFNames=CORT_0B06030 {ECO:0000313|EMBL:CCG22312.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG22312.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG22312.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
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; HE681720; CCG22312.1; -; Genomic_DNA.
DR   RefSeq; XP_003867749.1; XM_003867701.1.
DR   GeneID; 14538805; -.
DR   KEGG; cot:CORT_0B06030; -.
DR   eggNOG; KOG0560; Eukaryota.
DR   HOGENOM; CLU_001975_2_1_1; -.
DR   OrthoDB; 5474937at2759; -.
DR   Proteomes; UP000005018; Chromosome 2.
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   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
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   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}.
FT   DOMAIN          686..835
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   1443 AA;  161805 MW;  A52F5B7BED9A47A1 CRC64;
     MMSLSKEESI ARTVDLVDGV SFVTQPAKSV ESPYAKLVYN ANILINSNDP YAIVENFLLD
     RDNQRNDKRE DGIEEPDLDT VTVITDSETL LRNLPFLSAS SFKNNKVVNH VEINNKDFTV
     VTSLKDLNFP ILISQTPRET YQFANLAYNL SENLNTSVFH FYVSESSYKS NETIKTSEGV
     FLKSLQQLSF DKVLAEFDIH PFEVVNKIQK QKDAILYLGQ LDDALLEAAS KAGVLVINIK
     VYQPFSVSRL LKLVPAQIET LTLVQQAHSS FSQFSPLLLD FFAAYSEHQT LKNFTKIVSA
     AFGPVVDYTN AFTKVVSNVH SNKPYQNLFY GELERSNGSN KRHQEYEKAV SEAHNLEQAY
     LKILQQVNDT NLKILNEYQA DNIGLETNPE YGFGSFLYNE EQQENLVRLV QVALKENKFR
     TKDNNKLIDL LSQWLVQIQE NGEVENRIPL EAINLLKTDD SSTSSRELLA LSSYFTTNSN
     WLIGSDAWSY DLGSSGVHSV ITSGKNINML IIDSEPYKEK SSDKTVNGFR KKDVGLYAMN
     HGDCYVASVA VYSSYTQVLQ AFIEAEKFNG PSIILAYLPY HKESDDTLAV LQETKKAVDT
     GYWPLYRFDP NAAKETDVFK LDSSNLRKQL QDFLDKENKL TLLAAKDPLL SRNLTANANT
     EAKLKQAKIA DESYAMLLQG LSGPPLTIAF ASDGGNAEGL AKKINRQALG RGLKASVLAM
     DEISMEDLPN ETNIVFVTST SGQGEFPGNG KQFWDGLKNS NDLDLSGVRF SVFGLGDSEY
     WPRKEDKHYY NKPGKDLHAK LKLYGGVELA EIGLGDDQDA DGFSTGFNEW IPKIWAALGV
     DNVEGVEEPK PITNEDMKLG SDYLRGTIAE GLQDESTGSI CAVDQQLTKF HGIYMQDDRD
     VRDERKAQGL EPAYAFMVRV RLPGGIANPK QYLKMDELAD ERGNGTLKLT TRATFQLHGV
     VKHDLKPAIR GMNAALMDTL AACGDVNRNV MVSALPDNAK VHGQVSATGT LISNHLLPNT
     TAYHEIWLEG EMPSDKSGDR EAWENRKEGP TKKKTLVAGN VLADVEPLYG VTYLPRKFKI
     VITVPPYNDV DVYAHDIGLI AIVEDDIVTG YNVLVGGGMG TTHNNKKTYP RTGSMFGYIP
     RDQIHIACEK IMLVQRDFGD RSNRKHARLK YTIDDMGVEV YKSKVEDLLG YKFEEPRPFK
     IENNVDHFGW CKDELGYNHF TAFIENGRIE DTPELPQKTG LRKIAQYLQD NKKSGEFRLT
     GNQHILISNI KDEDLQDVRD LLAKYKLDNT EFSALRLSSA ACVAFPTCGL AMAESERYLP
     KLITKLEEAL EDYGLRHDSV VMRMTGCPNG CARPWVAEVA LVGKAYGAYN LMLGGGHHGQ
     RLNKIYRYSI KEDEILAILK DLFKRWSKER NDGEPFGDWC IRARIIQETT EGKYFHEGIP
     EDA
//