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Database: UniProt
Entry: B5LMU0_CHLPE
LinkDB: B5LMU0_CHLPE
Original site: B5LMU0_CHLPE 
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
//
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