ID A0A1V1UDD2_9RHOB Unreviewed; 332 AA.
AC A0A1V1UDD2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:GAW33701.1};
GN Name=gap_2 {ECO:0000313|EMBL:GAW33701.1};
GN ORFNames=RA2_00744 {ECO:0000313|EMBL:GAW33701.1};
OS Roseovarius sp. A-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1570360 {ECO:0000313|EMBL:GAW33701.1, ECO:0000313|Proteomes:UP000191225};
RN [1] {ECO:0000313|EMBL:GAW33701.1, ECO:0000313|Proteomes:UP000191225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-2 {ECO:0000313|EMBL:GAW33701.1,
RC ECO:0000313|Proteomes:UP000191225};
RA Harada M., Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H.,
RA Amachi S.;
RT "Genome sequencing of bacteria contributing to the geochemical cycling of
RT arsenic, bromine, and iodine.";
RL Submitted (NOV-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:GAW33701.1}.
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DR EMBL; BDIY01000002; GAW33701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1UDD2; -.
DR STRING; 1570360.RA2_00744; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000191225; 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 6..152
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 332 AA; 35997 MW; 559D5066B00CABD8 CRC64;
MPHAPIRIAM NGFGRIGRTL LRILMRDGGD FELVCINDIE PLATCAYLFQ YDSVFGPWPG
QVSTRDGVLI VDGHEIPFHS ERDLRALDLS GVDLVLECTG MGGKRAMAER GIEAGAHAVL
VSGPSAEADV TLVMGANDDD LRDQRIISNA SCTTNALAPL ARLLDEAYGI VSGQMTTVHC
YTGSQPTVDK PRDLPERSRA AALSMVPTTT SAQHQTGLVL PALKDRIEAR AIRVPTASVS
CIDLTVQTRE VVTLEAVNAM LHGAAQTRNW LGWTEDPVVS CDLRGRPESL VLSGPQTSVS
QGGLLRVFGW YDNEWGFSCR MLDMARRIAR RG
//
