ID   GPDM_CAEEL              Reviewed;         722 AA.
AC   P90795; Q22793;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Probable glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPDH-M;
DE            Short=GPD-M;
DE            EC=1.1.5.3;
DE   Flags: Precursor;
GN   ORFNames=T25G3.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- ENZYME REGULATION: Calcium-binding enhance the activity of the
CC       enzyme.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
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DR   EMBL; Z73906; CAA98123.1; -; Genomic_DNA.
DR   EMBL; Z72516; CAA98123.1; JOINED; Genomic_DNA.
DR   EMBL; Z72516; CAA96690.1; -; Genomic_DNA.
DR   EMBL; Z73906; CAA96690.1; JOINED; Genomic_DNA.
DR   PIR; T20362; T20362.
DR   RefSeq; NP_492115.1; -.
DR   UniGene; Cel.7665; -.
DR   HSSP; P02593; 1AK8.
DR   Ensembl; T25G3.4; Caenorhabditis elegans.
DR   GeneID; 172509; -.
DR   KEGG; cel:T25G3.4; -.
DR   NMPDR; fig|6239.3.peg.1942; -.
DR   WormBase; WBGene00012031; T25G3.4.
DR   WormPep; T25G3.4; CE14180.
DR   OMA; P90795; DSIRKMD.
DR   BRENDA; 1.1.99.5; 672.
DR   NextBio; 875825; -.
DR   ArrayExpress; P90795; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-Hand_type.
DR   InterPro; IPR018248; EF_hand.
DR   InterPro; IPR018247; EF_HAND_1.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca_bd.
DR   InterPro; IPR000447; FAD-dep_Gly3P_DH.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF00036; efhand; 2.
DR   PRINTS; PR01001; FADG3PDH.
DR   ProDom; PD000012; EF-hand; 1.
DR   SMART; SM00054; EFh; 2.
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   2: Evidence at transcript level;
KW   Calcium; Complete proteome; FAD; Flavoprotein; Mitochondrion;
KW   Oxidoreductase; Repeat; Transit peptide.
FT   TRANSIT       1     43       Mitochondrion.
FT   CHAIN        44    722       Probable glycerol-3-phosphate
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000010432.
FT   DOMAIN      624    659       EF-hand 1.
FT   DOMAIN      660    695       EF-hand 2.
FT   NP_BIND      76    104       FAD (Potential).
FT   CA_BIND     673    684       Potential.
SQ   SEQUENCE   722 AA;  80807 MW;  9E8BF74246480E30 CRC64;
     MSWVRFTKTG VAVVATSAAA VLALDMTNER RFQRQVKDHF RTVHADRLAE LNKRAPSALP
     TRKDILTNLS KGEEFDVLII GGGATGAGVA LDAQTRGLKT ALVELDDFSS GTSSRSTKLI
     HGGVRYLQAA IMKLDLEQYR MVKEALFERH NLLEIAPHLS SPLPIMLPIY KLWQVPYYWS
     GIKAYDFVSG KRVLKNSFFI NKSQALERFP MLRNESLKGA LIYYDGQHND ARMNLAIILT
     AIRHGAACAN HVRVEKLNKD ETGKVIGAHV RDMVTGGEWD IKAKAVINAT GPFTDSIRLM
     GDPETARPIC APSSGVHITL PGYYSPSNTG LLDPDTSDGR VIFFLPWERM TIAGTTDAPS
     DVTLSPQPTD HDIEFILQEI RGYLSKDVSV RRGDVMSAWS GLRPLVRDPN KKDTKSLARN
     HIIEVGKSGL ITIAGGKWTT YRHMAEETVD RVVEVHGLKT ENGCVTPGLL LEGAHDWNSL
     QYIHLVQDYG MEVDVAQHLS NTYGDRAFVV ARMCKMTGKR WPIVGQRLHP EFPYLDAEVR
     YAVREYACTA IDVIARRMRL AFLNTYAAHE VLPDVVRVMG QELGWSSAEQ RAQLEKARTF
     IDMEMGQNAK QTAVSNVALN LTKEEMQRAK ERFQQLDKDR KGHITVNDLR KHFREHNQKI
     DERVLHELLN EVDLNKNGEI EIAEFFQLYS GLKGGQLTGN RLVGYLDEIH GTPSVNRACG
     GI
//