ID H2AUZ8_KAZAF Unreviewed; 467 AA.
AC H2AUZ8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Fumarate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.1.6 {ECO:0000256|RuleBase:RU366062};
GN Name=KAFR0E00440 {ECO:0000313|EMBL:CCF58198.1};
GN ORFNames=KAFR_0E00440 {ECO:0000313|EMBL:CCF58198.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58198.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58198.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Irreversibly catalyzes the reduction of fumarate to
CC succinate. {ECO:0000256|RuleBase:RU366062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + succinate = fumarate + H(+) + NADH;
CC Xref=Rhea:RHEA:18281, ChEBI:CHEBI:15378, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.6;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC Note=Binds 1 FAD per monomer. {ECO:0000256|RuleBase:RU366062};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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DR EMBL; HE650825; CCF58198.1; -; Genomic_DNA.
DR RefSeq; XP_003957333.1; XM_003957284.1.
DR AlphaFoldDB; H2AUZ8; -.
DR STRING; 1071382.H2AUZ8; -.
DR GeneID; 13882675; -.
DR KEGG; kaf:KAFR_0E00440; -.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; H2AUZ8; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000005220; Chromosome 5.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; IEA:UniProtKB-EC.
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; 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:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU366062};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366062};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366062};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 4..449
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 467 AA; 50129 MW; F0D82917C709ECE2 CRC64;
MSAVVIIGSG LAGLTTANEL VSKNIPIILV DKASSIGGNS IKASSGINGA HTKTQLSLNI
ENDSPELFFN DTVKSAKGKG VEELMDKLSK DSKHAIEWLQ SEPFNIKLDL LAQLGGHSVP
RTHRSSGKLP PGFEIVSVLS KRLKDLAESN PDLVKIFLDS KVVDVKVNAQ NEVTGIEYEN
KDGENKTLDS NKVVFCSGGF SFSKEMLSKY APDLVKLPTT NGAQTTGDGQ RILEKLGADM
IDMDQIQVHP TGFIDPADRT CAWKFLAAEA LRGLGGILLN PSTGKRFVNE LSTRDVVTDA
IQTQGPKEEN RSLLVMGEGI YDVLKNNLDF YMFKKLVKKV TLKEVVDNFK LPITAEELAQ
ELTQYQTNSA DQYGRALVTK NFGENINAHT SVFIGEVTPV VHFTMGGAKI NSKAEVVNKD
GSILAKGLYA AGEVSGGVHG ANRLGGSSLL ECVVFGRTAA ASISESA
//
