GPDM_MACFA
ID GPDM_MACFA Reviewed; 727 AA.
AC Q4R755;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE Short=GPD-M;
DE Short=GPDH-M;
DE EC=1.1.5.3 {ECO:0000250|UniProtKB:P43304};
DE AltName: Full=mtGPD;
DE Flags: Precursor;
GN Name=GPD2; ORFNames=QtsA-16270;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-responsive mitochondrial glycerol-3-phosphate
CC dehydrogenase which seems to be a key component of the pancreatic beta-
CC cell glucose-sensing device. {ECO:0000250|UniProtKB:P43304}.
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:0000250|UniProtKB:P43304};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC Evidence={ECO:0000250|UniProtKB:P43304};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Calcium-binding enhance the activity of the
CC enzyme. {ECO:0000250|UniProtKB:P43304}.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
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; AB168970; BAE01068.1; -; mRNA.
DR RefSeq; NP_001306361.1; NM_001319432.1.
DR AlphaFoldDB; Q4R755; -.
DR SMR; Q4R755; -.
DR STRING; 9541.XP_005573274.1; -.
DR GeneID; 102127260; -.
DR CTD; 2820; -.
DR eggNOG; KOG0042; Eukaryota.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd00051; EFh; 1.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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 Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; FAD; Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 43..727
FT /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"
FT /id="PRO_0000270069"
FT DOMAIN 623..658
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 659..694
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71..99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 683
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 601
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64521"
SQ SEQUENCE 727 AA; 80801 MW; CFB9E66271721B66 CRC64;
MAFQKAVKGT ILVGGGALAT VLGLSQFAHY RRKQMNLAYV KAADYISEPV NREPPSREAQ
LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI VLPVYKWWQL PYYWVGIKLY
DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
AATANYMEVV SLLKKTDPQT GKVRVSGARC KDVLTGQEFD VRAKCVINAT GPFTDSVRKM
DDKDAAAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD
VTPHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH
VVDISESGLI TIAGGKWTTY RSMAEDTINA AIKTHNLKAG PSRTVGLFLQ GGKDWSPTLY
IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDHKKQE QLETAKKFLY
YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADKK GFITIVDVQR VLESINVQMD
ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
DRSCGGL