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Database: UniProt
Entry: L1LD33_THEEQ
LinkDB: L1LD33_THEEQ
Original site: L1LD33_THEEQ 
ID   L1LD33_THEEQ            Unreviewed;       614 AA.
AC   L1LD33;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN   ORFNames=BEWA_052440 {ECO:0000313|EMBL:EKX73189.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX73189.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:EKX73189.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:EKX73189.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:EKX73189.1}.
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DR   EMBL; ACOU01000003; EKX73189.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1LD33; -.
DR   STRING; 1537102.L1LD33; -.
DR   EnsemblProtists; EKX73189; EKX73189; BEWA_052440.
DR   VEuPathDB; PiroplasmaDB:BEWA_052440; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   OrthoDB; 989271at2759; -.
DR   Proteomes; UP000031512; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0004369; F:glycerol-3-phosphate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
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   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EKX73189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512}.
FT   DOMAIN          60..432
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          462..596
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   614 AA;  67879 MW;  1727A23150644C6A CRC64;
     MGRKCRNLIG ICSGAIAGSY LFVKREHEKC SLPRDTKFII PDKLKSRSDM IKSLKSDKFD
     VLVIGGGCTG TSVALDCATR GLKCALVEAN DFSSGTTSKS TKLLHGGIRY LESALLHLDL
     KELQFVWKAL EERAHLIGTA PFANSPVPIV MPIYQLWQLP YFWINIKIYE VLARFFCCNE
     TRIPSSFFSG KSNAVFNFPG IRPDGLLGAV VYYDGQHNDS RTNVLMALTS TIDEYVPGQV
     GSTIGNYLKV EELLKDSTGK VNGALVCDVL TGETFTVKAD VVVNCAGPFA EKIKKLSLPE
     SKLNILHSRG THVTLPAKYC PTPYGLIIPK TSDGRVLFIL PWQGNTIVGT TDNKDELQAN
     PLPQVQDVDF ICKDASKYMN CDASQIKADI KSTWSGLRPL LKGVDEVNQT GKLSRGHVIE
     VDESGLVNVY GGKWTICRLM AQECVDKVVK HFPSVTKGSY ACRTRNMVLL GTHNKEGVSD
     IDDIKPRFNR LSSVITEKYG LDSTVSNHLV ESYGYKALDV CELSKEMGLL KPIHEEHPYI
     MGEVVYGIRN EMACKPIDIL ARRTRLAFKD VHAAVSSLGL VCDLMGKELS WSAETREQLH
     KEATAYLKDM MVPS
//
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