ID A0A1S9ZP66_9GAMM Unreviewed; 362 AA.
AC A0A1S9ZP66;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:OOR85246.1};
GN ORFNames=B0180_00140 {ECO:0000313|EMBL:OOR85246.1};
OS Moraxella canis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR85246.1, ECO:0000313|Proteomes:UP000190322};
RN [1] {ECO:0000313|EMBL:OOR85246.1, ECO:0000313|Proteomes:UP000190322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR85246.1,
RC ECO:0000313|Proteomes:UP000190322};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOR85246.1}.
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DR EMBL; MUXT01000001; OOR85246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9ZP66; -.
DR Proteomes; UP000190322; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD 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 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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 NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 15..181
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 24..25
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 208
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 362 AA; 39657 MW; 8116E0733A47E545 CRC64;
MIPNNSHRQA DTPKLRLAIN GFGRIGRNVL RAYIKKLGVF DNIDIVAIND IADNEVLLHL
LKFDSTHGRF DQGDNAAQVS LTTDQDTSYL TITKGGSSRR ILLLSCDEPE NLPWKDLDVD
VVLECTGQFR SYADANRHRT AGAKQVIIGA APFDSVDASI VIGVNDDELN ADLPIISGVS
CTTQALVPLL SVLDDKFGIQ SAMMTEIHAV TADQSVLDQA HRDFRRARAS GHNIIPTTSS
SINATERVLP LMRGKINGHS IRVPTINVAA IDLTVKFAQS VRLDEIKDAL MTASQGHLVG
IMDYCDEPLV SSDFIGDSHS LVIDGQQLMM AGELAKIYAW YDNEWGYANR LLDMCQKLAG
LR
//
