ID   A4I397_LEIIN            Unreviewed;       608 AA.
AC   A4I397; A0A2K4YY59; A0A381MN33;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 2.
DT   27-MAR-2024, entry version 91.
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=LINJ_28_0240 {ECO:0000313|EMBL:CAM69251.2};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM69251.2, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM69251.2, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM69251.2,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM69251.2, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM69251.2,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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}.
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DR   EMBL; FR796460; CAM69251.2; -; Genomic_DNA.
DR   RefSeq; XP_001470059.2; XM_001470022.2.
DR   AlphaFoldDB; A4I397; -.
DR   SMR; A4I397; -.
DR   STRING; 5671.A4I397; -.
DR   GeneID; 5070244; -.
DR   KEGG; lif:LINJ_28_0240; -.
DR   VEuPathDB; TriTrypDB:LINF_280007300; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   InParanoid; A4I397; -.
DR   OMA; PHIVKPM; -.
DR   OrthoDB; 989271at2759; -.
DR   Proteomes; UP000008153; Chromosome 28.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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   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   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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT   DOMAIN          69..411
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          471..590
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   608 AA;  66642 MW;  C9007B39F2A4B893 CRC64;
     MAATAVKYVI GAGVAVFGGM VGFSYTNPAW TQRRFDTSKC PPLKYETVPT REMCVQALKA
     HNSVTNPLDV LIIGGGCVGA GSALDAVTRG LSVGMVDMGD YAGETSSRST KLIHGGIRYL
     QKAVFQADPM QLKLVAEALR ERTIMIHQAP HLCHSLPTLV PCYHPIDIGM YWCGAKMYDL
     MAAFYGGTLE YSSFLFPYEV MKAYPKLRKM DQDNNALLGA VRYYDGQMND ARLCYSVAMT
     AACYGAATVN YARVKQMEVV KDDKGDELVR AIIEESIARK TIEVYSRSII NAGGPFSGEV
     EKLAKGAERQ LDMFPAAGTH IVIDRKYCPR EREAMVVPSN DGRVVFAIPW LGGCLLGTTD
     HTCDVQSNPP VPQADVDFLL ENIRPFIGSV PPEAVKSAWT GIRPLAIPKA QKLRGGGTQN
     IVREHVIAVD PKSHVLNITG GKWTTYRKMA EEAVDELQRT LMKGKADFKP CCTMNLVLVG
     ARNLDKVAST APLGIPEDVH KHWRSNYGDR YGEVMAVATK DSKLMARLAK DSPVVEAEVV
     YAAQGEHCEH VMDFIARRTR IAFVNAEQAE QVVPRVTELM GQVKGWGNSK RNAERAAAYS
     ALASFQGR
//