GPDM_DICDI
ID GPDM_DICDI Reviewed; 638 AA.
AC Q54QC1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable glycerol-3-phosphate dehydrogenase, mitochondrial;
DE Short=GPD-M;
DE Short=GPDH-M;
DE EC=1.1.5.3;
DE Flags: Precursor;
GN ORFNames=DDB_G0283951;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AAFI02000058; EAL65463.1; -; Genomic_DNA.
DR RefSeq; XP_638823.1; XM_633731.1.
DR AlphaFoldDB; Q54QC1; -.
DR SMR; Q54QC1; -.
DR STRING; 44689.DDB0185769; -.
DR PaxDb; Q54QC1; -.
DR PRIDE; Q54QC1; -.
DR EnsemblProtists; EAL65463; EAL65463; DDB_G0283951.
DR GeneID; 8624347; -.
DR KEGG; ddi:DDB_G0283951; -.
DR dictyBase; DDB_G0283951; -.
DR eggNOG; KOG0042; Eukaryota.
DR HOGENOM; CLU_015740_4_1_1; -.
DR InParanoid; Q54QC1; -.
DR OMA; CIVNAAG; -.
DR PhylomeDB; Q54QC1; -.
DR Reactome; R-DDI-1483166; Synthesis of PA.
DR Reactome; R-DDI-163560; Triglyceride catabolism.
DR UniPathway; UPA00618; UER00673.
DR PRO; PR:Q54QC1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; -; 1.
DR Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..638
FT /note="Probable glycerol-3-phosphate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000355967"
FT BINDING 100..128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 638 AA; 71425 MW; 19DA700617840BBC CRC64;
MNQLLSKSFK PLVVAGVAVI GISAFSGNRA YDEYRKERES ISKKMINDLN ENKITMFDYF
QECKTLGRDE QLSKLNKLSK VYNKQKLNEQ ENQEELIDLD LIVIGGGATG TGVALDAQSR
GMKVALFEKY DFSSGTSSKS TKLVHGGIRY LESAIMKLKP SELTLVKEAL RERSNLLNNA
PHLSRQLPIV IPAYSIFDAS KFWIGCKLYD FFYPFNDIPK SYLQTSAQTY KEFPFLREGL
VSSVVYYDGQ HNDSRMNVSL ALTAAQQGAL TLNYTEVVEL IKDDKINNNN KQQQLKGVVI
RDRLTGKKYS VPAKCVVNAT GPYCDSIRNL DDPRADPIIT ASSGVHIMLP GNLIPSDKGF
LNPKTKDGRV LFILPFEGKT LVGTTDDPSP IIENPQPLEK DVEFILDSIK EYSNPNVKLD
KSQVLACWSG IRPLVSDEPA AQGDNKKSTS QVTRSHSLRM SESGLITIVG GKWTTYRSMA
EATVNLVCSK HDIFTPKGCI TKNLPLIGGE KYYNTLNQYL IKNFNLPEDI AEHLAHSYGD
QAPFVAKLAN ENGSNKRLVE GYPYIEAEVT YGVKKEYACT AEDIIGRRTR LSFLDHDKAE
IALPKIINIM APLLKWSNER KKEELKNSQN YLKTMTSK
