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Database: UniProt
Entry: F9FYM4_FUSOF
LinkDB: F9FYM4_FUSOF
Original site: F9FYM4_FUSOF 
ID   F9FYM4_FUSOF            Unreviewed;      1609 AA.
AC   F9FYM4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN   ORFNames=FOXB_11506 {ECO:0000313|EMBL:EGU77988.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU77988.1};
RN   [1] {ECO:0000313|EMBL:EGU77988.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU77988.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU77988.1}.
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DR   EMBL; AFQF01002890; EGU77988.1; -; Genomic_DNA.
DR   STRING; 660025.F9FYM4; -.
DR   PaxDb; 5507-FOXG_13941P0; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR005330; MHYT_dom.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   Pfam; PF03707; MHYT; 2.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
DR   PROSITE; PS50924; MHYT; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217}; Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        54..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..218
FT                   /note="MHYT"
FT                   /evidence="ECO:0000259|PROSITE:PS50924"
FT   REGION          409..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1609 AA;  178152 MW;  EC9F7EC34A03F902 CRC64;
     MSTEELLQRY QGHIVPQSYN AGFVALSYVV SLVGAGSTLE LINRRTGLRG LFNHLLLMSS
     AVTMGGVSIW CMHFIGNRAI DLADGQPELQ VAYSSGFTAI SFFVPIIVLL AAFMAVGTNN
     VVSWWRLVAG GVLCGTAVCG MHYLGNASIN NYTCVYQPSY VIGSAIIAIV ASNVALAMFF
     VFRAMWANAW WKRVISAVVL AGAVSGMHWC ASVGTRYRLK RIKPNGNEPS RTGTVVVVIC
     LSLGACFIIA TSAILRARNM RRSALRAQQI TLAAAVFDKG GRILVDPDGY IPSTVVTDSF
     LEKQNAKEGF NTGHSLFHWM YQASRNWNMI WSLVGGMRQH VSQLPHSRTH KDGRRGIQLV
     SEHGETIDSY DMIFRELFCL AAAALADRLR EDLTSIGVLW DQILPTGANG RRPRPQLRKQ
     SNAGTGLEGS DANEEVHNSL DITEKGLHVE NHDYGRGSLM FLVRRSESVR DTERLISTGY
     RFAELHQVSD LIKSSMQIKT HDFETKLREM ATYTSERNHI RQGTHLGFFA VRARVSSGFE
     VLVRKGARHL LPSMPFPFEN LEDWQMHYLR RFENVPVSKI VEKCKEDSQR SDREAEFAGQ
     IADTIKELRE STQEPLLEDA LLTSTAFRIP CRGDEKRLEA TMIAVRLVIP IHSVLSSPNC
     EFVPLSFFRM RQVSTQAYQE FTRGLHQEFG HIAKTAKRQE GSQDKISPSL SSRWPFGRSE
     TTRSTRTRGK SLSRISGHVV SSNDSARSSS TINLCSPGTN ARTQSIDSGE GSSTYVPRQE
     PLQATPSYGG IMVFQEITVD VQEGGETAAR KPSHGSEVDT ITIERTISKP SAAAGIELQS
     MGHFGANDIG TQLSNDIEAG ICICLYLTLH ICPSWFQSKY HTPSSSRYRT KSLNKLPLKV
     VLLPQMPAFA GAPRGLIRRF WLPGVVTTSA AVLIYSYRPR DFTGHTSPAV PPPTFGADGT
     FKLPRFPRVK TREEQLDQLR GSSRPQVQQY DILVIGGGAT GAGVALDAAT RGLKVAVVER
     DDFSSGTSSK STKLVHGGVR YLEKAVWNLD YNQYLLVKEA LKERKYFLQT APHLSSWLPI
     MLPLDKWWKA PYYWAGTKFY DFLAGSEGIE GSYFLTRSKA LEAFPMLKPT DLVGALVYYD
     GAHNDSRMNV SIAMTAALYG ATVVNHAEVT GLIKNGDGNL CGAIVRDLVS VKDGRPAEVI
     TVRAKSVINC TGPFTDSVRK MDDPGCKEIV APASGVHVIL PGYFSPGKMG LIDPSTSDGR
     VIFFLPWQGN TIAGTTDSPS TITPNPLPDE KSIEWILSEI SHYLSPEINV RRGDVLAAWS
     GIRPLVKDPK AKNTESLVRN HLIDISASGL LTCAGGKWTT YRQMAEECVD FAIQEFRLEP
     RPVADAPRVS GTDLIDDGAI LDGKCQTHKV RLLGAHGFSP TLFIPIIQHF GVETEVAKHL
     TESYGDRAWT VASLCKLTDK RFPARGERIS QLYPFVDGEI RYAIRHEYAQ TAVDVLARRT
     RLAFLNAQAA LEALPKVIDI MAEELKWSRQ RKDLEWKECA YYGQFPIPSV SAMTRLPHSH
     KPLAVAYLES MGLPKPMLTV TRKQVEQGKL DFASSLEWQM YSRHDKPTD
//
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