ID A0A0D5YTW4_9FLAO Unreviewed; 336 AA.
AC A0A0D5YTW4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase, type I {ECO:0000313|EMBL:AKA35772.1};
GN ORFNames=VC82_2179 {ECO:0000313|EMBL:AKA35772.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA35772.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA35772.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA35772.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; CP011071; AKA35772.1; -; Genomic_DNA.
DR RefSeq; WP_045802389.1; NZ_CP011071.1.
DR AlphaFoldDB; A0A0D5YTW4; -.
DR STRING; 516051.VC82_2179; -.
DR KEGG; mlt:VC82_2179; -.
DR PATRIC; fig|516051.4.peg.2244; -.
DR HOGENOM; CLU_030140_0_2_10; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000032726; Chromosome.
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:0006006; P:glucose metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032726}.
FT DOMAIN 4..153
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 336 AA; 37539 MW; DF71ACC148713A2A CRC64;
MPQINIGING FGRIGRTLFR LLQKHPDFRV VALNDLGNAQ TLAHLLKYDS LHGVFDGEIK
AEGNAIWVND RKTQVLNHEH PKDINWKQYE VDLVVEASGK FKNRSALEHH LKNGAKKVFL
SVPPEDDTIK MVVIGVNEDI LAPTDDIISN ASCTTNNAAP MIKVIHELCG IEQAYITTVH
SYTSDQSLHD RPHRDLRRSR AAGQSIIPTT TGAAKALTKI FPELSNAIGG CGIRVPVPNG
SLTDITFNVK RETSIDEINS TFKKVSENEQ KNVLFYTEDP IVSVDINNSC YSCTFDSQMT
SVIGRMVKII GWYDNETGYC SRMIDLIELL IKNRYI
//
