ID A0A091CWZ5_FUKDA Unreviewed; 796 AA.
AC A0A091CWZ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00020025};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN ORFNames=H920_16106 {ECO:0000313|EMBL:KFO22410.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO22410.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO22410.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO22410.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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:0000256|ARBA:ARBA00003074}.
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|ARBA:ARBA00001590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC Evidence={ECO:0000256|ARBA:ARBA00001590};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation.
CC {ECO:0000256|ARBA:ARBA00004745}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; KN124048; KFO22410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CWZ5; -.
DR STRING; 885580.ENSFDAP00000003186; -.
DR eggNOG; KOG0042; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:InterPro.
DR CDD; cd00051; EFh; 1.
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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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; PF13499; EF-hand_7; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 692..727
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 728..763
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 796 AA; 89089 MW; 8D471484A215796C CRC64;
MNTGETVHSI GIVHADQVNL AYVEAAECFE PVNREPPSRE AQLLTLRNTS EFDILVIGGG
ATGSGCALDA VTRVLLLGSP SCCSDLRYSQ GLSKKQPLSF LGRFKHFPLL KLMLAIDTCL
IHANCYDDHD HPSIHSAYSE EPLPRDSWKL RTWLLLFLNI GLKTALVERD DFSSGTSSRS
TKLIHGGVRY LQKAIMKLDI EQYRMVKEAL HERANLLEIA PHLSAPLPIM LPVYKWWQLP
YYWVGIKLYD LVAGSNCLKS SYVLSKSRAL EHFPMLQKDR LVGAIVYYDG QHNDARMNLA
IALTAARYGA ATANYMEVVS LLKKTDPETG RERVSGARCK DVLTGQEFDV RAKCVINATG
PFTDAVRKMD DKSATAICQP SAGVHIVMPG YYSPESMGLL DPATSDGRVI FFLPWQKMTI
AGTTDSPTDI THHPIPSEED INFILNEVRN YLSCDVEVRR GDVLAAWSGI RPLVTDPKSA
DTQSISRNHV VDISESGLIT IAGGKWTTYR SMAEDTVNAA IKVHDLKAGP SRTVGLFLQG
GKDWSPTLYI RLVQDYGLES EVAQHLAATY GDKAFEVAKM ASVTGKRWPI VGVRLVSEFP
YIEAEVKYGI KEYACTAVDM ISRRTRLAFL NVQAAEEALP RIVELMGREL NWDEKKKEKE
LETARRFLYY EMGYKSRSEQ LTDRSEISLL PSDIDRYKKR FHKFDADQKG FITIVDVQRV
LESINVQMDE NTLHEILNEV DLNKNGQVEL NEFLQLMSAI QKGRVSGSRL AILMKTAEEN
LDRRVPIPVD RSCGGL
//
