ID W2SJ07_NECAM Unreviewed; 720 AA.
AC W2SJ07;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN ORFNames=NECAME_05425 {ECO:0000313|EMBL:ETN68836.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN68836.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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|RuleBase:RU361217};
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}.
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DR EMBL; KI669191; ETN68836.1; -; Genomic_DNA.
DR RefSeq; XP_013291063.1; XM_013435609.1.
DR AlphaFoldDB; W2SJ07; -.
DR STRING; 51031.W2SJ07; -.
DR EnsemblMetazoa; NECAME_05425; NECAME_05425; NECAME_05425.
DR GeneID; 25345457; -.
DR KEGG; nai:NECAME_05425; -.
DR CTD; 25345457; -.
DR OMA; GVMTIMN; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000053676; 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: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:UniProtKB-UniRule.
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 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; PS00977; FAD_G3PDH_1; 1.
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 ECO:0000256|RuleBase:RU361217};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 622..657
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 658..693
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 720 AA; 80347 MW; 14C89A54A14DBE2A CRC64;
MFASRLAKAG AVVGLSAAAV LTLDVTNERR FRRQMKQYFR TAHADKLADL NKRPSTALPS
RKEIIESLKA NEEFDVLIIG GGATGAGVAL DAQTRGLKTA LVELDDFSSG TSSRSTKLIH
GGVRYLQAAI MKADFEQYRM VKEALFERAN LLEIAPHLSA PLPIMLPVYK LWQVPYYWAG
IKAYDFVSGK RVLKNSFYIN KTKAMERFPM LKSDSLKGAL IYYDGTHNDA RMNLAIVLTA
IRHGAKCVNH TKVERLLKDE DGKVVGAHVR DMMTGNEWDI KAKSIVNATG PSTDTIRLMA
DPQTKPICAP SSGVHIVLPG YYSPSNTGLL DPDTSDGRVI FFLPWERMTI AGTTDAPSEV
TLSPIPKDSD VEFILQEIRG YLSKDVSVRR GDVMSSWSGL RPLVRDPNKK DTKSLARNHI
IEVSESGLVT IAGGKWTTYR HMAEETVDTC VKAKNLDPTN GCITAGLMLE GGHEYNPLMY
IHLVQDYGLE VDVAQHLANT YGDRAFVVAR MCKMTGKRWP IIGNRLHQEF PYLDAEVRYA
VREYACTAVD VIARRTRLAF LNTYAAHEVL PEVVRIMAEE LGWSSAEQRS QLERARQFID
LEMGQLAKQN AASSVSLNLT SEEMQAAKDR FNKLDKDKKG HITVNDLRRH FREHNQKIDE
RVLHELLNEV DLNKNGEIEI AEFFQLYSGL KGGQISANRL VRYLDEMHGT PSVSRSGGGV
//
