ID B5LMU0_CHLPE Unreviewed; 335 AA.
AC B5LMU0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=gap {ECO:0000313|EMBL:ACH42161.1};
GN OrderedLocusNames=G5S_0421 {ECO:0000313|EMBL:AEB41419.1};
OS Chlamydia pecorum (strain ATCC VR-628 / DSM 29919 / E58) (Chlamydophila
OS pecorum).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=331635 {ECO:0000313|EMBL:ACH42161.1};
RN [1] {ECO:0000313|EMBL:ACH42161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E58 {ECO:0000313|EMBL:ACH42161.1};
RA Mohamad K.Y., Roche S.M., Myers G., Bavoil P.M., Laroucau K., Magnino S.,
RA Laurent S., Rasschaert D., Rodolakis A.;
RT "Preliminary phylogenetic identification of virulent Chlamydophila pecorum
RT strains.";
RL Vet. Res. 0:0-0(2008).
RN [2] {ECO:0000313|EMBL:ACH42161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E58 {ECO:0000313|EMBL:ACH42161.1};
RA Myers G.S., Read T.D., Brunham R.C., Kaltenboeck B., Bavoil P.;
RT "Genome Sequence of Chlamydophila pecorum E58.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEB41419.1, ECO:0000313|Proteomes:UP000008305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-628 / E58 {ECO:0000313|Proteomes:UP000008305}, and E58
RC {ECO:0000313|EMBL:AEB41419.1};
RX PubMed=21571992; DOI=10.1128/JB.00454-11;
RA Mojica S., Huot Creasy H., Daugherty S., Read T.D., Kim T., Kaltenboeck B.,
RA Bavoil P., Myers G.S.;
RT "Genome sequence of the obligate intracellular animal pathogen Chlamydia
RT pecorum E58.";
RL J. Bacteriol. 193:3690-3690(2011).
RN [4] {ECO:0000313|EMBL:AEB41419.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E58 {ECO:0000313|EMBL:AEB41419.1};
RA Mojical S., Drabek E.F., Huot Creasy H., Daugherty S., Read T.D.,
RA Kaltenboeck B., Bavoil P., Myers G.S.A.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC NAD. The first reaction step involves the formation of a hemiacetal
CC intermediate between G3P and a cysteine residue, and this hemiacetal
CC intermediate is then oxidized to a thioester, with concomitant
CC reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC second NAD, and the thioester is attacked by a nucleophilic inorganic
CC phosphate to produce BPG. {ECO:0000256|ARBA:ARBA00003501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001810};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; EU837074; ACH42161.1; -; Genomic_DNA.
DR EMBL; CP002608; AEB41419.1; -; Genomic_DNA.
DR RefSeq; WP_013712497.1; NC_015408.1.
DR AlphaFoldDB; B5LMU0; -.
DR KEGG; cpm:G5S_0421; -.
DR OMA; TCRIEKG; -.
DR Proteomes; UP000008305; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 1..151
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 335 AA; 36437 MW; 93E30C92D7F31AF5 CRC64;
MNVVINGFGR IGRLVLRQIL KRNSNLQVLA VNDLVPGDAL AYLFKYDSTH GRFSSEVSYE
DGCLISGKQK IRFLAERDVQ KLPWKELGVD VVVESTGLFT KKEDAAKHLE SGTKRVLISA
PAKGDVPTFV MGVNHHAYNP ATDLIISNAS CTTNCLAPIA KVLLDNFGIE EGLMTTVHAA
TATQPVVDGP SKKDWRGGRS ALQNIIPAST GAAKAVALCL PELKNKLTGM AFRVPVADVS
VVDLTVRLAK STTYEEICSA MKHSSETNLK GILGYTDEEV VSSDYIGSEF SSIFDSLAGI
ALNDRFFKLV SWYDNEIGYA TRIVDLLEYV AQNSK
//