ID Q5AKX2_CANAL Unreviewed; 648 AA.
AC Q5AKX2;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Fumarate reductase {ECO:0000313|EMBL:AOW26969.1};
GN Name=OSM2 {ECO:0000313|CGD:CAL0000192083,
GN ECO:0000313|EMBL:AOW26969.1};
GN OrderedLocusNames=CAALFM_C113670WA {ECO:0000313|EMBL:AOW26969.1},
GN orf19.12472 {ECO:0000313|CGD:CAL0000192083};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW26969.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW26969.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW26969.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW26969.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP017623; AOW26969.1; -; Genomic_DNA.
DR RefSeq; XP_722209.1; XM_717116.1.
DR AlphaFoldDB; Q5AKX2; -.
DR SMR; Q5AKX2; -.
DR STRING; 237561.Q5AKX2; -.
DR EnsemblFungi; C1_13670W_A-T; C1_13670W_A-T-p1; C1_13670W_A.
DR GeneID; 3636193; -.
DR KEGG; cal:CAALFM_C113670WA; -.
DR CGD; CAL0000192083; OSM2.
DR VEuPathDB; FungiDB:C1_13670W_A; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; Q5AKX2; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
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; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
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; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR PANTHER; PTHR43400:SF8; HYPOTHETICAL FUMARATE REDUCTASE (EUROFUNG); 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000000559}.
FT DOMAIN 564..640
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 516..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70459 MW; 396AC4BF741210BF CRC64;
MSTASIPSNP ILIVGGGLAG LSAAHQAYLR GANVVLLDKE SFLSGNSGKA TSGINGALTR
TQVNLKIPDS VEQFYQDTLA SAKDRAHPEL IKVLTYNSAD AVHWLQEVFD LDLTVVSRLG
GHSQPRTHRG HDAKFPGMAI TYRLLERLET LSETEPDRVV ILKNSQVIDL IMEQDNKVVG
VKYKNLKDKS KHELYGPVIL STGGYAADFT KNSLIRKYRP DIIDLPSTNG GHATGDGQKI
VQKNKGQVLD MDKIQVHPTG LISYKDKDIV ERKKTPRFLF LGAEALRGEG GIIFNSKGER
FVDELGTRDW VSGEMDKQIK QGNFPIRLVL SEKAGENLKF HVKHYTQRGL MRTVSGKELV
EEMGCSEDIV KQQLDTYNKA ASGAIKDPFG KKYFPATPFE YSPDAKYHVS FITPVLHFTM
GGVKINDKTQ VIADNDSPFE GLYAAGEVAG GVHGHNRLGG SSLLACVVYG RLAADQASSY
KFHKLSFGDG DSIASASQRL KMINLHIDPS NGRIFIDTNG NGGEGNTAST STPDNGGSSS
SAAAPPPPPQ KKAPKQPKPF SVPDKEFTAE EVAQHNKPGD CWCIIKNVVL DLTPFLGDHP
GGKESIANFA GRDATESFAM LHDDDFIPKY VANCVLGRLK GKTSELQL
//
