ID   GPDM_MESAU              Reviewed;         727 AA.
AC   A7DZP8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=mGPD;
DE   Flags: Precursor;
GN   Name=GPD2;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Venkatesh K., Shivaji S.;
RT   "Hamster sperm capacitation: role of FAD linked glycerol-3-phosphate
RT   dehydrogenase.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM774032; CAO79918.1; -; mRNA.
DR   RefSeq; NP_001268609.1; NM_001281680.1.
DR   AlphaFoldDB; A7DZP8; -.
DR   SMR; A7DZP8; -.
DR   STRING; 10036.XP_005069035.1; -.
DR   GeneID; 101825992; -.
DR   CTD; 2820; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   OrthoDB; 669193at2759; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000189706; 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   1: Evidence at protein 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_0000355968"
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;  80857 MW;  89C18A4C8D0205DA CRC64;
     MAFQKAVKRT VLVCGGALAT VLGLSQCSHY RRKQVNLACL KAAGCHTEPV NREPPSREAQ
     LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
     YLQKAIMKLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPIYKWWQL PYYWVGIKLY
     DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
     AATANYREVV SLLKKTDPET GKERVSGARC KDVLTGLEFD VRAKCVINAT GPFTDSVRKM
     DDNKAPAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWENMT IAGTTDSPTK
     NTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVIDPKS ADTQSISRNH
     VVDVSESGLI TIAGGKWTTY RSMAEDTVDT AIKVHNLKAG PCRTVGLFLQ GGKDWSPTLY
     IRLVQDYGLE SEVAQHLATT YGDKAFEVAK MAKVTGKRWP IVGVRLVSEF PYIEAEVKYG
     IKEYACTAVD MISRRTRLAF LNIQAAEEAL PRIVELMGRE LDWSEIRKQA ELETATKFLY
     YEMGSKSRSE QLTDRTEISL RPSDIERYTK RFHKFDADEK GFITIVDVQR VLENINVKID
     ENTLHEILSE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
     DRSCGGL