ID A0A3P3DMW5_9RHOB Unreviewed; 326 AA.
AC A0A3P3DMW5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:RRH75515.1};
GN ORFNames=EG244_08505 {ECO:0000313|EMBL:RRH75515.1};
OS Falsigemmobacter faecalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Falsigemmobacter.
OX NCBI_TaxID=2488730 {ECO:0000313|EMBL:RRH75515.1, ECO:0000313|Proteomes:UP000282125};
RN [1] {ECO:0000313|EMBL:RRH75515.1, ECO:0000313|Proteomes:UP000282125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102744-1 {ECO:0000313|EMBL:RRH75515.1,
RC ECO:0000313|Proteomes:UP000282125};
RA Li G., Jiang Y.;
RT "Gemmobacter sp. nov., YIM 102744-1 draft genome.";
RL Submitted (NOV-2018) 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:RRH75515.1}.
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DR EMBL; RRAZ01000010; RRH75515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3DMW5; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000282125; 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 1..149
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 149
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 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 326 AA; 34626 MW; 63EC0A69560EDEEE CRC64;
MRVALNGMGR IGRTVLRAWI TGRWPGIEIV ALNDIASAED VAYLTEFDSV FGVFPGEVRL
EEGHLLVAGR RLRLTRAADL STLDLSDIDL VMECTGRADT PEVAARGLRA GAGRVLISGP
SEAAEFTVVL GANEEALRRS HKIVSNASCT TNALAPLLRV LEETVGVESG WMTTIHCYTG
SQPTVDAPRG APARSRAAAL SMVPTTTSAG HLVDVVLPQI AGRVSCAAVR VPVASVSAID
LSFHPRHHGT AAEINAILQS AGGVIGWTNK PLVSSDLRAR PESVVMALPE TVVTGGGIVR
VFGWYDNEWG FSCRMLDVAS LWERAV
//