ID A0A178GGA1_9GAMM Unreviewed; 340 AA.
AC A0A178GGA1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:OAL83499.1};
GN ORFNames=AY605_10650 {ECO:0000313|EMBL:OAL83499.1};
OS Acinetobacter sp. SFD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL83499.1, ECO:0000313|Proteomes:UP000186186};
RN [1] {ECO:0000313|EMBL:OAL83499.1, ECO:0000313|Proteomes:UP000186186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFD {ECO:0000313|EMBL:OAL83499.1,
RC ECO:0000313|Proteomes:UP000186186};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAL83499.1}.
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DR EMBL; LSZJ01000014; OAL83499.1; -; Genomic_DNA.
DR RefSeq; WP_064096634.1; NZ_LSZJ01000014.1.
DR AlphaFoldDB; A0A178GGA1; -.
DR STRING; 1805635.AY605_10650; -.
DR Proteomes; UP000186186; 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:SF3; D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43148; 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 2..162
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 189
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 340 AA; 37716 MW; 8BECD6D217EA1F4A CRC64;
MQRVAINGFG RIGRNVLRAW FENPKDFNFE IVAINDIADV ETLIHLFKYD STHGRFSGQV
DLSYDAEHIY LHISYKDAAL KVQVLCEAEP AKLPWQNLAV DVVLECTGLF RSREAATQHI
QAGAKRVIIG AAPFDTVDAA IVYGVNHHEV KASDQIISSV SCTTQALVPL VKIVDDAFGI
NSALMTEIHA VTADQSVLDH AHRDLRRARA SGHNIIPTTS SALGALKRVM PKMEDRIDGY
SIRVPTINVA AIDLTFVSQS PITDHKLNEV LIKAARQDFA EIMAVTDEPL VSSDFNHSPY
SLIVDLTQTL VVGHQAKVFA WYDNEWGYAN RLLDLCESFH
//
