ID K1PSB1_CRAGI Unreviewed; 624 AA.
AC K1PSB1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CGI_10007865 {ECO:0000313|EMBL:EKC24513.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC24513.1};
RN [1] {ECO:0000313|EMBL:EKC24513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC24513.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000256|ARBA:ARBA00006235}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH816071; EKC24513.1; -; Genomic_DNA.
DR AlphaFoldDB; K1PSB1; -.
DR HOGENOM; CLU_438230_0_0_1; -.
DR InParanoid; K1PSB1; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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 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; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049337; TOR1A_C.
DR InterPro; IPR010448; Torsin.
DR PANTHER; PTHR10760:SF2; LD13476P-RELATED; 1.
DR PANTHER; PTHR10760; TORSIN; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF21376; TOR1A_C; 1.
DR Pfam; PF06309; Torsin; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 374..513
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 624 AA; 70778 MW; 254C60C5B1B49F8F CRC64;
MSVTQTLAEY ETGLDHGEFK LDWNFLGEDE NVSKKPTTSP NECTDNSIAL NTPAPNIPEC
SVFPETSATV HSEEEPMSKR PRFPTRKVSV TLKKGNAPSR TDRKEISQVP NVSAMEDQLK
YAWSPLPTRQ NMIDSLKKDE FDVLVIGGGA TGCGVALDAV SRGLKTGLVE KFDFSSGTSS
RSTKLIHGGV RYLQKAVFNL DIEQVPYFWA GIKTYDVIAG KQLLKPSYYL SKRKALELFP
MLKKEKLVGA LVYYDATMVA RRKVKDMNMM GKVWGRRIVS LLGKKRMAEY PFVRLSAIEP
FSALGAIGTA VVAGLYTVFT PIKCQFKECC TSKWISLNTT ALQEDLRRRL YGQHLVTDVI
IKHLKSHMTK DPSKALTLSF HGGTGTGKNY VSKIIAESIY KEGMRSKYVH LISATKEFPH
KDMVPLYKDK LRNLVESSVN ECPQSLFIFD EIDKMPAGIL DTLKPYFDFY EQLGGTDYRR
AMFIFLSNTA GEDISKHALN NWRSKEFKRE DIGLKEMEQI ISTAAINSKT SKYSTICGMY
HSDIIYKHMI TAYVPFLPME RKHIKECIKD LLVARNYYRR EDIPEDKIRV IAQELNYYPA
DMEIFSVTGC KRVPEKVTYV MDEE
//
