ID A0A1L0BQ19_9ASCO Unreviewed; 559 AA.
AC A0A1L0BQ19;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=CIC11C00000002610 {ECO:0000313|EMBL:SGZ53339.1};
GN ORFNames=SAMEA4029010_CIC11G00000002610 {ECO:0000313|EMBL:SGZ53339.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ53339.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ53339.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ53339.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; LT635759; SGZ53339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0BQ19; -.
DR STRING; 45354.A0A1L0BQ19; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000182334; Chromosome iv.
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; cd02922; FCB2_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000182334}.
FT DOMAIN 68..146
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 172..533
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 559 AA; 61382 MW; 2A705CD068C2804E CRC64;
MFSKRLVARI ARVKTPKVSR GSRGLSSSRY VSPTISLKSR VSLALVSCTL SALAVAWSNE
SVDLDSLAPG VPVEEVEKHN SVENGVWVVI NGKVYNLTEF LTRHPGGAKI ILKYAGKDAL
AIFNKFHAPN FVDKYLTPEE CLGPLIGEME VAPDVTEAGD DTQRLENIKN KPPISEVFRV
SDFEYIARKI LPPTAWCYYS SGADDEISLR ENHNAFSRIF FKPRVLVDVS SVDVSTIMMG
EATEVPFYCS AAAQAKLGHP DGELSIARGC GKEGVIQMIS NYSSYPLEDI VDAASKGQPQ
WFQLYVTDHE SARESVDECN ELGLKSIFVT VDTPELGRRE KDMKLRAQIL AQMDDSDESA
DSQESLDLGS SVVYGRDTAV TWKDITEITN WTDIPVAVKG VQSVEDVVLA AENGVKAVVI
SNHGGRQLDY ARAPIEVLAD TIPVLKEKGL DDKIEIYIDG GVRRGSDIIK CLALGAKGVG
LGRIFLYANA AYGEEGVRKA CQMLKEEIKL DMRLLGVSKI SELGPQHLDL RNLYSRNPPA
DNLYNNNYEP LSPPAFKSE
//