GLPO_MYCPN
ID GLPO_MYCPN Reviewed; 384 AA.
AC P75063;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glycerol 3-phosphate oxidase {ECO:0000303|PubMed:19028882};
DE Short=GlpO {ECO:0000303|PubMed:25688572, ECO:0000303|PubMed:25712468};
DE EC=1.1.3.21 {ECO:0000269|PubMed:19028882, ECO:0000269|PubMed:25712468};
DE AltName: Full=L-alpha-glycerophosphate oxidase {ECO:0000303|PubMed:25688572, ECO:0000303|PubMed:25712468};
DE Flags: Precursor;
GN Name=glpD {ECO:0000303|PubMed:19028882, ECO:0000312|EMBL:AAB95751.1};
GN OrderedLocusNames=MPN_051; ORFNames=D09_orf384, MP103;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP INDUCTION, AND PATHWAY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=19028882; DOI=10.1128/jb.01103-08;
RA Hames C., Halbedel S., Hoppert M., Frey J., Stuelke J.;
RT "Glycerol metabolism is important for cytotoxicity of Mycoplasma
RT pneumoniae.";
RL J. Bacteriol. 191:747-753(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP REACTION MECHANISM.
RX PubMed=25712468; DOI=10.1111/febs.13247;
RA Maenpuen S., Watthaisong P., Supon P., Sucharitakul J., Parsonage D.,
RA Karplus P.A., Claiborne A., Chaiyen P.;
RT "Kinetic mechanism of L-alpha-glycerophosphate oxidase from Mycoplasma
RT pneumoniae.";
RL FEBS J. 282:3043-3059(2015).
RN [4] {ECO:0007744|PDB:4X9M, ECO:0007744|PDB:4X9N}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FAD AND
RP GLYCEROL-3-PHOSPHATE, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=25688572; DOI=10.1111/febs.13233;
RA Elkhal C.K., Kean K.M., Parsonage D., Maenpuen S., Chaiyen P.,
RA Claiborne A., Karplus P.A.;
RT "Structure and proposed mechanism of L-alpha-glycerophosphate oxidase from
RT Mycoplasma pneumoniae.";
RL FEBS J. 282:3030-3042(2015).
CC -!- FUNCTION: Catalyzes the oxidation of glycerol 3-phosphate to
CC dihydroxyacetone phosphate (DHAP), with a reduction of O2 to H2O2. The
CC formation of hydrogen peroxide by this enzyme is crucial for cytotoxic
CC effects of M.pneumoniae on host cells. Is involved in the metabolism of
CC glycerol and is essential for glycerol utilization; glycerol is one of
CC the few carbon sources that can be utilized by M.pneumoniae for growth
CC (PubMed:19028882). To a lesser extent, is also able to use
CC glyceraldehyde 3-phosphate (GAP), an intermediate in the glycolysis
CC pathway, as a substrate (but the structure of the product has not been
CC elucidated). Therefore, in the absence of glycerol, GAP may serve as a
CC substrate in the GlpO reaction to supply H2O2 during mycoplasma
CC infection (PubMed:25712468). Does not show any dehydrogenase activity
CC with NAD(+) (PubMed:19028882). {ECO:0000269|PubMed:19028882,
CC ECO:0000269|PubMed:25712468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate +
CC H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642; EC=1.1.3.21;
CC Evidence={ECO:0000269|PubMed:19028882, ECO:0000269|PubMed:25712468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18370;
CC Evidence={ECO:0000269|PubMed:19028882};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19028882, ECO:0000269|PubMed:25712468};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 mM for sn-glycerol 3-phosphate (at pH 7 and 4 degrees Celsius)
CC {ECO:0000269|PubMed:25712468};
CC KM=55 uM for O2 (at pH 7 and 4 degrees Celsius)
CC {ECO:0000269|PubMed:25712468};
CC KM=12 mM for sn-glycerol 3-phosphate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:25712468};
CC KM=1.8 mM for D/L-glyceraldehyde 3-phosphate (at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:25712468};
CC Note=kcat is 4.2 sec(-1) with sn-glycerol 3-phosphate as substrate
CC (at pH 7 and 4 degrees Celsius). kcat is 60.1 sec(-1) with sn-
CC glycerol 3-phosphate as substrate (at pH 7 and 25 degrees Celsius).
CC kcat is 0.6 sec(-1) with sn-glycerol 3-phosphate as substrate (at pH
CC 7 and 25 degrees Celsius). {ECO:0000269|PubMed:25712468};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000269|PubMed:19028882}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25688572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19028882}. Cell
CC membrane {ECO:0000255|PROSITE-ProRule:PRU00303,
CC ECO:0000269|PubMed:19028882}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Note=Is present predominantly in the cytoplasm, but
CC a few proteins can also be detected at the cell surface.
CC {ECO:0000269|PubMed:19028882}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:19028882}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow at all in
CC glycerol-containing medium, and exhibit a significantly reduced
CC formation of hydrogen peroxide and a severely reduced cytotoxicity.
CC {ECO:0000269|PubMed:19028882}.
CC -!- MISCELLANEOUS: The reaction mechanism follows a ping-pong model; after
CC flavin-mediated substrate oxidation, DHAP leaves rapidly prior to the
CC oxygen reaction that reoxidizes the flavin and produces H2O2.
CC {ECO:0000269|PubMed:25712468}.
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DR EMBL; U00089; AAB95751.1; -; Genomic_DNA.
DR PIR; S73429; S73429.
DR RefSeq; NP_109739.1; NC_000912.1.
DR RefSeq; WP_010874408.1; NC_000912.1.
DR PDB; 4X9M; X-ray; 2.40 A; A=1-384.
DR PDB; 4X9N; X-ray; 2.50 A; A=1-384.
DR PDBsum; 4X9M; -.
DR PDBsum; 4X9N; -.
DR AlphaFoldDB; P75063; -.
DR SMR; P75063; -.
DR IntAct; P75063; 1.
DR STRING; 272634.MPN_051; -.
DR EnsemblBacteria; AAB95751; AAB95751; MPN_051.
DR KEGG; mpn:MPN_051; -.
DR PATRIC; fig|272634.6.peg.51; -.
DR HOGENOM; CLU_024775_3_0_14; -.
DR OMA; GVHFTRM; -.
DR BioCyc; MPNE272634:G1GJ3-74-MON; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; FAD; Flavoprotein;
KW Glycerol metabolism; Lipoprotein; Membrane; Oxidoreductase; Palmitate;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..384
FT /note="Glycerol 3-phosphate oxidase"
FT /id="PRO_0000210396"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:25688572"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 47..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 47
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0007744|PDB:4X9M"
FT BINDING 51
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0007744|PDB:4X9M"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 258
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0007744|PDB:4X9M"
FT BINDING 320
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0007744|PDB:4X9M"
FT BINDING 346..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT BINDING 348
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0007744|PDB:4X9M"
FT BINDING 352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:25688572,
FT ECO:0007744|PDB:4X9M"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4X9M"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 311..323
FT /evidence="ECO:0007829|PDB:4X9M"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:4X9M"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:4X9M"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:4X9M"
SQ SEQUENCE 384 AA; 42724 MW; DA3E128719EE1BCD CRC64;
METRDVLIVG GGVIGCATAY ELSQYKLKVT LVEKHHYLAQ ETSHANSGVI HTGIDPNPHK
LTAKYNILGK KLWLNTYFKR LGFPRQKIRT LIVAFNEMER EQLEVLKQRG IANQINLEDI
QMLSKEETLK LEPYVNPEIV AGLKIEGSWA IDPVLASKCL ALAAQQNKVQ ICTNTEVTNI
SKQVDGTYLV WTNNETTPSF KVKKIIDAAG HYADYLAHLA KADDFEQTTR RGQYVVVTNQ
GELHLNSMVF MVPTIHGKGV IVSPMLDGNF LVGPTALDGV DKEATRYITK DAPCMLTKIG
KHMVPSLNIN NALISFAGSR PIDKATNDFI IRVAHNDPDF VILGGMKSPG LTAAPAIVRE
AVRLLNWKLT KKPNWNGKYN LPWI
