ID A0A091TP10_PHALP Unreviewed; 507 AA.
AC A0A091TP10;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00020025};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
DE Flags: Fragment;
GN ORFNames=N335_12439 {ECO:0000313|EMBL:KFQ79406.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ79406.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ79406.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ79406.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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; KK461513; KFQ79406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TP10; -.
DR PhylomeDB; A0A091TP10; -.
DR Proteomes; UP000053638; 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; 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; 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 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:UP000053638};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 403..438
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 439..474
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ79406.1"
FT NON_TER 507
FT /evidence="ECO:0000313|EMBL:KFQ79406.1"
SQ SEQUENCE 507 AA; 56340 MW; 30E5B3D6CC820592 CRC64;
GQHNDARMNL AIALTAARYG AATANYAEVL RLLKTTDPAS GKERVCGVRC RDVLTGQEFD
VKAKCVINAT GPFTDSVRKM DDQEVQNICQ PSAGVHIVMP GYYSPDNMGL LDPATSDGRV
IFFLPWEKMT IAGTTDSPTD VTSHPIPTEE DINFILNEVR NYLSVDVEVR RGDVLAAWSG
IRPLVTDPNS KDTQSISRNH VVTISDSGLV TIAGGKWTTY RAMAQDTIDA AIQAHDLKAG
SSKTIGLQLQ GAEDWSPTLY IRLVQDYGLE SEVAQHLAST YGDKAFEVAK IAQVTGKRWP
IVGKRLVSEF PYIEAEVVYG VKEYARTAVD MISRRTRLAF LNVQAAEEAL PRIVDIMGKE
LNWNEQKKKE ELEAAKRFLY YEMGYKVKSD QLTDSSEISL APSDIERYKK RFHMFDKDKK
GFITILDVQR VLESISVQIA ENTLHDILNE VDLNKNGQVE LNEFLQLMSA IQKGHVSGSR
LAVLMKTAEE NLHQRLVIPV DRSGGGL
//
