ID A0A093BK39_CHAPE Unreviewed; 348 AA.
AC A0A093BK39;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
DE Flags: Fragment;
GN ORFNames=M959_13674 {ECO:0000313|EMBL:KFU86963.1};
OS Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC Apodinae; Chaetura.
OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU86963.1, ECO:0000313|Proteomes:UP000031515};
RN [1] {ECO:0000313|EMBL:KFU86963.1, ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M959 {ECO:0000313|EMBL:KFU86963.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25504712; DOI=10.1126/science.1251385;
RG Avian Genome Consortium;
RA Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT "Comparative genomics reveals insights into avian genome evolution and
RT adaptation.";
RL Science 346:1311-1320(2014).
CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity.
CC {ECO:0000256|ARBA:ARBA00037527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC Evidence={ECO:0000256|ARBA:ARBA00001343};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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DR EMBL; KN126158; KFU86963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093BK39; -.
DR Proteomes; UP000031515; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF32; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)], CYTOPLASMIC; 1.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Reference proteome {ECO:0000313|Proteomes:UP000031515}.
FT DOMAIN 5..172
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 195..339
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 269..270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT NON_TER 348
FT /evidence="ECO:0000313|EMBL:KFU86963.1"
SQ SEQUENCE 348 AA; 37737 MW; 6CE5143E831D9D7F CRC64;
MGGKKVCIVG SGNWGSAIAK IAGSNAARLS GFESQVRMWV LQEEVGGRRL TDIINTEHEN
VKYLPGHKLP PNVVAEPDLL KACAEADILL FVVPHQFIGK VCDQLQGHVK KNAVGMSLIK
GVDEGPDGLR LISDIIHEKL GIEMSVLMGA NIANEVAEEK FCETTIGCKN LQHGQMLKEL
MQTPNFRVTV VEEADTVEIC GALKNVVAVG AGFCDGLGYG DNTKAAVIRL GLMEMIGFAK
LFCKGPVTSS TFLQSCGVAD LITTCYGGRN RRVAEAFAKT GKSIEQLEKE MLNGQKLQGP
QTSAELHRIL KSKNVVEKFP LFTAVYQICY EGKPVTDVIK CLQNHPEH
//
