G1PDH_AERPE
ID G1PDH_AERPE Reviewed; 352 AA.
AC Q9YER2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+];
DE Short=G1P dehydrogenase;
DE Short=G1PDH;
DE Short=Gro1PDH;
DE EC=1.1.1.261 {ECO:0000269|PubMed:11846799};
DE AltName: Full=Enantiomeric glycerophosphate synthase;
DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase;
GN Name=egsA; OrderedLocusNames=APE_0519.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=11846799; DOI=10.1046/j.0014-2956.2001.02731.x;
RA Han J.-S., Kosugi Y., Ishida H., Ishikawa K.;
RT "Kinetic study of sn-glycerol-1-phosphate dehydrogenase from the aerobic
RT hyperthermophilic archaeon, Aeropyrum pernix K1.";
RL Eur. J. Biochem. 269:969-976(2002).
RN [3]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, METAL-BINDING SITES, AND
RP MUTAGENESIS OF ASP-126; ASP-173; HIS-253 AND HIS-269.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=15876564; DOI=10.1155/2005/257264;
RA Han J.-S., Ishikawa K.;
RT "Active site of Zn(2+)-dependent sn-glycerol-1-phosphate dehydrogenase from
RT Aeropyrum pernix K1.";
RL Archaea 1:311-317(2005).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of
CC dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-
CC phosphate (G1P). The G1P thus generated is used as the glycerophosphate
CC backbone of phospholipids in the cellular membranes of Archaea. Is also
CC able to catalyze the reverse reaction, i.e. the NAD(+)-dependent
CC oxidation of G1P but not of G3P. Is not active toward glycerol,
CC dihydroxyacetone, glyceraldehyde phosphate, and glycerol-2-phosphate.
CC {ECO:0000269|PubMed:11846799, ECO:0000269|PubMed:15876564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:57945; EC=1.1.1.261;
CC Evidence={ECO:0000269|PubMed:11846799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.261;
CC Evidence={ECO:0000269|PubMed:11846799};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15876564};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15876564};
CC -!- ACTIVITY REGULATION: Totally inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:15876564}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for DHAP (in the presence of NADH as coenzyme)
CC {ECO:0000269|PubMed:11846799};
CC KM=0.29 mM for DHAP (in the presence of NADPH as coenzyme)
CC {ECO:0000269|PubMed:11846799};
CC KM=0.032 mM for NADH {ECO:0000269|PubMed:11846799};
CC KM=0.044 mM for NADPH {ECO:0000269|PubMed:11846799};
CC KM=8.92 mM for G1P {ECO:0000269|PubMed:11846799};
CC KM=1.57 mM for NAD(+) {ECO:0000269|PubMed:11846799};
CC Temperature dependence:
CC Optimum temperature is 94-96 degrees Celsius. Over 96 degrees
CC Celsius, the activity decreases dramatically. Hyperthermostable. The
CC half-life of activity is 30 minutes at 95 degrees Celsius and
CC increases to 2 hours at 90 degrees Celsius.
CC {ECO:0000269|PubMed:11846799};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11846799}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Catalysis proceeds by an orered bi-bi kinetic mechanism.
CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BA000002; BAA79484.2; -; Genomic_DNA.
DR PIR; H72748; H72748.
DR AlphaFoldDB; Q9YER2; -.
DR SMR; Q9YER2; -.
DR STRING; 272557.APE_0519.1; -.
DR EnsemblBacteria; BAA79484; BAA79484; APE_0519.1.
DR KEGG; ape:APE_0519.1; -.
DR PATRIC; fig|272557.25.peg.391; -.
DR eggNOG; arCOG00982; Archaea.
DR SABIO-RK; Q9YER2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106357; F:glycerol-1-phosphate dehydrogenase [NAD+] activity; IEA:RHEA.
DR GO; GO:0106358; F:glycerol-1-phosphate dehydrogenase [NADP+] activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1.
DR InterPro; IPR023002; G1P_dehydrogenase_arc.
DR InterPro; IPR032837; G1PDH.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; NAD; NADP; Oxidoreductase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Zinc.
FT CHAIN 1..352
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000157338"
FT BINDING 99..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT MUTAGEN 126
FT /note="D->A: 4-fold and 2-fold increase in activity when
FT NADH and NADPH are used as cosubstrate, respectively.
FT Decrease in affinity for NAD and DHAP, but increase in NADP
FT affinity. No effect on zinc ion affinity."
FT /evidence="ECO:0000269|PubMed:15876564"
FT MUTAGEN 126
FT /note="D->N: 12-fold and 3-fold increase in activity when
FT NADH and NADPH are used as cosubstrate, respectively. 2- to
FT 9-fold decrease in affinity for substrates. No effect on
FT zinc ion affinity."
FT /evidence="ECO:0000269|PubMed:15876564"
FT MUTAGEN 173
FT /note="D->N: Decrease in activity and in affinity for
FT substrates and zinc ion. Loss of activity and zinc binding;
FT when associated with A-253."
FT /evidence="ECO:0000269|PubMed:15876564"
FT MUTAGEN 253
FT /note="H->A: Decrease in activity and in affinity for
FT substrates. Loss of activity and zinc binding; when
FT associated with N-173."
FT /evidence="ECO:0000269|PubMed:15876564"
FT MUTAGEN 269
FT /note="H->A: Decrease in activity and in zinc ion
FT affinity."
FT /evidence="ECO:0000269|PubMed:15876564"
SQ SEQUENCE 352 AA; 37667 MW; 47E7CA60E02FEDD7 CRC64;
MYTSFHRIDL PRTIVVGGGV LDKAGGYVSG VAQRGSYVLV VSGPTVSSKY FERLRASLEA
EGLTVGLKII RDATVETAEE VAREALESRI EVVAGLGGGK SIDVAKYASK RAGSVFVSIP
TVASHDGITS PFSSLKGFDK PISRPAKAPE AIIIDVDVIA EAPRRYNIAG FGDLIGKYTA
VLDWRLAHKL RLEYYGEYAA SLALLSAKHV SQYAEEIALG TREGYRVLLE ALVSSGVSMC
IAGSTRPASG SEHLFAHALH IVARNKPLHG EAVGVGTIMM AYLHGKNWRR IRGLLKTVGA
PTNAKELGVE DDEVVEALTI AARIRPERYT ILGEKGLTRE AAEALARKTG VI
