GPDA_COXBU
ID GPDA_COXBU Reviewed; 332 AA.
AC Q83BJ0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
DE EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; OrderedLocusNames=CBU_1518;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00394};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00394};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
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DR EMBL; AE016828; AAO91015.1; -; Genomic_DNA.
DR RefSeq; NP_820501.1; NC_002971.3.
DR RefSeq; WP_010958277.1; NZ_CCYB01000022.1.
DR PDB; 3K96; X-ray; 2.10 A; A/B=1-332.
DR PDBsum; 3K96; -.
DR AlphaFoldDB; Q83BJ0; -.
DR SMR; Q83BJ0; -.
DR STRING; 227377.CBU_1518; -.
DR EnsemblBacteria; AAO91015; AAO91015; CBU_1518.
DR GeneID; 1209428; -.
DR KEGG; cbu:CBU_1518; -.
DR PATRIC; fig|227377.7.peg.1521; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_2_6; -.
DR OMA; NRMFGNM; -.
DR UniPathway; UPA00940; -.
DR EvolutionaryTrace; Q83BJ0; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IBA:GO_Central.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 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; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD;
KW Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000137953"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3K96"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3K96"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3K96"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:3K96"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 182..204
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 209..229
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3K96"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:3K96"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:3K96"
SQ SEQUENCE 332 AA; 36067 MW; 0790551553B52A94 CRC64;
MEPFKHPIAI LGAGSWGTAL ALVLARKGQK VRLWSYESDH VDEMQAEGVN NRYLPNYPFP
ETLKAYCDLK ASLEGVTDIL IVVPSFAFHE VITRMKPLID AKTRIAWGTK GLAKGSRLLH
EVVATELGQV PMAVISGPSL ATEVAANLPT AVSLASNNSQ FSKDLIERLH GQRFRVYKND
DMIGVELCGS VKNILAIATG ISDGLKLGSN ARAALITRGL TEMGRLVSVF GGKQETLTGL
AGLGDLVLTC TDNQSRNRRF GLALGEGVDK KEAQQAIGQA IEGLYNTDQV HALAQKHAIE
MPLTFQVHRI LHEDLDPQQA VQELLERSPK AE
