ID A0A1Y0N2L8_9FLAO Unreviewed; 480 AA.
AC A0A1Y0N2L8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ARV16776.1};
GN ORFNames=BTO07_17215 {ECO:0000313|EMBL:ARV16776.1};
OS Polaribacter sp. SA4-12.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV16776.1, ECO:0000313|Proteomes:UP000195470};
RN [1] {ECO:0000313|EMBL:ARV16776.1, ECO:0000313|Proteomes:UP000195470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-12 {ECO:0000313|EMBL:ARV16776.1,
RC ECO:0000313|Proteomes:UP000195470};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; CP019334; ARV16776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N2L8; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000195470; Chromosome.
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; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000195470}.
FT DOMAIN 130..292
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 480 AA; 53107 MW; C45622598E19685B CRC64;
MATILNYEDE VLSQAQNRRA TVEFITIVND LWYDKSIELV LFRNPLVDKR ASEVLNLISY
AKEFVSKPIS IQDALDIAKA IQQIDLPSSK LDIGKLAYEC HLNPEKGADK VAFVKDKLKG
ATKSVDIQPK DVVLYGFGRI GRLLARELMT KMGKGSQLRL RAIVTRGEIN QTVLEKRASL
LSIDSVHGDF LGTVETDVEN NALIINGTTV HMISAKQPED IDYTKFGIKD ALIIDNTGAF
RDDVALKRHL VAKGASKVLL TAPGKGIPNI VHGVNHKEHN PDNVDIFSAA SCTTNAITPI
LKVLEDNFGI KKGHLETIHA YTNDQNLVDN MHSKYRRGRA AALNMVITET GAGAAVAKAI
PALKDKLTSN AIRVPVPNGS LAILNLQLRT MVSKERVNAI IKKYALEGDL VEQIKYSLDN
ELVSSDIIGS TAPSIFDSKA TIADKETIVI YIWYDNEYGY SHQVMRLAKH IAKVRRFTYY
//
