ID A0A1V4K5B6_PATFA Unreviewed; 1088 AA.
AC A0A1V4K5B6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=GPD2 {ECO:0000313|EMBL:OPJ79658.1};
GN ORFNames=AV530_002161 {ECO:0000313|EMBL:OPJ79658.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ79658.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ79658.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ79658.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ79658.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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 ECO:0000256|RuleBase:RU361217};
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 ECO:0000256|RuleBase:RU361217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ79658.1}.
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DR EMBL; LSYS01004331; OPJ79658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4K5B6; -.
DR STRING; 372326.A0A1V4K5B6; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00051; EFh; 1.
DR CDD; cd06969; NR_DBD_NGFI-B; 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; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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 InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
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 Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01001; FADG3PDH.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00399; ZnF_C4; 1.
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 SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 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.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 239..314
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 984..1019
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1020..1055
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 139..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 485..512
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1088 AA; 119382 MW; 2681D3798A40A2CB CRC64;
MNGAVRVLCL DLCDNRVVNG SRGCCVRDVA EASQTSIAIN VYLHSGALTA VKAGRRWTRL
SASALGRLDS PENASPSAEA MPCVQAQYGS SPQGASPASQ SYSYHSSGEY SSDFLTPDFS
TFMDNYNTSY DSEEMMSHSG SVYYKPSSPP TPSTPGFQQS PPGTPVSSCQ MRFDGPLHVP
MNPEPAGPHH AVDGQAFAVP NPIRKQPSMA FPGLQLGHAP QLLDSQVPSP PSRGSPSNEG
LCAVCGDNAA CQHYGVRTCE GCKGFFKRTV QKNAKYVCLA NKNCPVDKRR RNRCQYCRFQ
KCLAVGMVKE VVRTDSLKGR RGRLPSKPKS PQEPSPPSPP VSLISALVRA HVDSNPAMTS
LDYSRKAVKG TALIGGGAIA TVFGLSQFSQ YRNKHGAFAH VQAAEAVTVP VKNHLPTREE
QILALRSTDE FDVLVIGGGA TGCGCALDAV TRGLKTALVE RDDFSSGTSS RSTKLIHGGV
RYLQKAIMKL DLEQYRMVKE ALEERANLLE IAPHLSSPLP IMLPVYKWWQ LPYYWLGIKL
YDMVAGSQCL KSSYVLSKSR ALELFPMLRK DELVAAIVYY DGQHNDARMN LAIALTAARY
GAATANYAEV LRLLKRTDPA GGKERVCGVR CRDVLTGQEF DVKAKCVINA TGPFTDSVRK
MDDQEVPNIC QPSAGVHIVM PGYYSPDHMG LLDPATSDGR VIFFLPWEKM TIAGTTDSPT
DVTSHPSPTE EDINFILNEV RNYLSVDVEV RRGDVLAAWS GIRPLVTDPN SKDTQSISRN
HVVTISDSGL VTIAGGKWTT YRAMAQDALD AAVEAHSLRA GSSRTIGLQL EGAEDWSPTL
YIRLVQDYGL ESEVAQHLAS TYGGKAYEVA KIAQVTGKRW PVVGKRLVSE FPYIEAEVVY
GVREYARTAV DMISRRTRLA FLNVQAAEEA LPRIVDIMGK ELHWSEQKKK EELEAAKKFL
YYEMGYKVKT DQLTDSSEIS LLPSDIERYE KRFHMFDKDK KGFITILDVQ RVLESIGVQI
AENTLHEILN EVDLNKNGQV ELNEFLQLMS AIQKGHVSGS RLAVLMKTAE ENLRRRVLIS
VDRSGGGL
//
