ID E1ZX09_CAMFO Unreviewed; 585 AA.
AC E1ZX09;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN ORFNames=EAG_02260 {ECO:0000313|EMBL:EFN74279.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN74279.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL434948; EFN74279.1; -; Genomic_DNA.
DR AlphaFoldDB; E1ZX09; -.
DR STRING; 104421.E1ZX09; -.
DR InParanoid; E1ZX09; -.
DR OMA; PHIVKPM; -.
DR Proteomes; UP000000311; 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:InterPro.
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; 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 Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 444..479
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 514..549
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 585 AA; 65883 MW; 56375CDF8088B9AB CRC64;
MYDLVAGSKT VKSSYYLSKS NALELFPMLK GDKLTGAIVY YDGQQDDARM NLAIALTASR
HGATVVNHVK VVNLLKGLDK DGKRVLVGAH LKDELTGEEW DVKAKAIINA TGPFTDHIRK
MDDQNVESIC APSSGVHIVL PGYYSPDQMG LLDPATSDGR VIFFLPWQKQ TIAGTTDLPC
EVTHNPRPTE DEIMFILQEV KNYLNPDVEV RRGDVLSAWS GIRPLVSDPN KPNTQSLARN
HIVHVSPTNL VTIAGGKWTT YRAMAQETID ATIKACDLQP ERSCQTDGFL LEGAQGWSPT
MYIRLVQDFG LECEVAQHLS KSYGDRAFAV AKMASLTGKR WPIIGKKIHP EFPYIDAEIR
YGVREYARTA IDMIARRLRL AFLNVQAAQE ALPAIIDIMA EELHWSTEEK KKQHREASEF
LAQEMGQMVN RASRDKIPIN LTKDEIQLYI KRFGIIDKDK KGYVSINDIR RGLKVLGIRM
NQDEMHSLLN EIDLTYNGQM ELQDYLQLFG DKEVPGEELH EILREIDTNM NGQVELDEYL
QMMSAIKSGH VAYSRFARMA EMEEAQHEKE MLKKQISVER SGGGL
//
