ID A0A2G8RCG8_9RHOB Unreviewed; 349 AA.
AC A0A2G8RCG8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:PIL19237.1};
GN ORFNames=P775_15735 {ECO:0000313|EMBL:PIL19237.1};
OS Puniceibacterium antarcticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1206336 {ECO:0000313|EMBL:PIL19237.1, ECO:0000313|Proteomes:UP000231259};
RN [1] {ECO:0000313|EMBL:PIL19237.1, ECO:0000313|Proteomes:UP000231259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1211 {ECO:0000313|EMBL:PIL19237.1,
RC ECO:0000313|Proteomes:UP000231259};
RA Zhang X.-Y., Liu C., Chen X.-L., Xie B.-B., Qin Q.-L., Rong J.-C.,
RA Zhang Y.-Z.;
RT "Genome sequencing of Phaeobacter antarcticus sp. nov. SM1211.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:PIL19237.1}.
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DR EMBL; AWWI01000106; PIL19237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RCG8; -.
DR Proteomes; UP000231259; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0006096; P:glycolytic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01546; GAPDH-II_archae; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000231259}.
FT DOMAIN 1..147
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
SQ SEQUENCE 349 AA; 37776 MW; F10915BAE9F12E90 CRC64;
MIGKRVADAV VAQEDMDLVG VADVTSDWRA RMARAVGVAD VTSDWRARMA RAKGFALYAA
DPDRTPAMRE AGLDVAGGLD DLLATADIVV DSTPKKVAVR NVETYRERGI RFIVHGGEKH
EVTGHSFVAE ANYASAIGRD RTRVVSCNTT SIVRTLTALK VAGLLGSARG TLLRRATDPW
ESHLGGIMNT LVPEPDIPSH QGPDAQSVDP DLDVITMAVK VPQTLAHLHY WSVRMPRKAS
KDEVLEAFRA SSRIALIRMA DGLGALNAVK EMMADFGRPN DSLYEVALWE DMLKVEGDEL
YYAYMVDNQA IVIPETIDAI RALTEAERDG SASIARTNAA LGVGTFTAT
//
