ID B0REX8_CLAMS Unreviewed; 357 AA.
AC B0REX8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394,
GN ECO:0000313|EMBL:CAQ02144.1};
GN OrderedLocusNames=CMS2048 {ECO:0000313|EMBL:CAQ02144.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02144.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ02144.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00394, ECO:0000256|RuleBase:RU000439};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}.
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DR EMBL; AM849034; CAQ02144.1; -; Genomic_DNA.
DR RefSeq; WP_012299368.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0REX8; -.
DR STRING; 31964.CMS2048; -.
DR KEGG; cms:CMS2048; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_2_11; -.
DR OrthoDB; 9812273at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001318; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
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:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00394};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00394}.
FT DOMAIN 28..184
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 204..343
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 32..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 279..280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ SEQUENCE 357 AA; 37305 MW; 4D6F85CF83680CA5 CRC64;
MSDATASPTP APAASTPDPD EGGERRRVVV LGAGSWGTTF AKVMADGGSD VVMWARRPEL
AREITEAKRN SDYLPGINLP QRLSAHPSLE RVLAGATDVF VSVPSQTLRA NLEAARDLIP
QDAVVVSLMK GVEKGTGLRM SEVIQEVLGI GPERIAVASG PNLALEIARE QPTAVVVSSA
EQATAERVAK IARSAYFRSF VNTDVIGTEF GGVLKNLIAV AVGIVDGVGY GENTKASIIT
RGLAEMTAFS VAYGARAETL AGLAGLGDLI ATCESSLSRN NTAGRLLGQG YSFTDVVKSM
QQTAEGLSSV APVLELARQR GVLMPIVEQV SQVLAGTLSP RDIAPHLTTD DDTPQGE
//
