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Database: UniProt
Entry: A0A1M6EUZ9_MALRU
LinkDB: A0A1M6EUZ9_MALRU
Original site: A0A1M6EUZ9_MALRU 
ID   A0A1M6EUZ9_MALRU        Unreviewed;       335 AA.
AC   A0A1M6EUZ9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=SAMN02745165_01040 {ECO:0000313|EMBL:SHI89160.1};
OS   Malonomonas rubra DSM 5091.
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Geopsychrobacteraceae; Malonomonas.
OX   NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHI89160.1, ECO:0000313|Proteomes:UP000184171};
RN   [1] {ECO:0000313|EMBL:SHI89160.1, ECO:0000313|Proteomes:UP000184171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5091 {ECO:0000313|EMBL:SHI89160.1,
RC   ECO:0000313|Proteomes:UP000184171};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQZT01000003; SHI89160.1; -; Genomic_DNA.
DR   RefSeq; WP_072906382.1; NZ_FQZT01000003.1.
DR   AlphaFoldDB; A0A1M6EUZ9; -.
DR   STRING; 1122189.SAMN02745165_01040; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000184171; Unassembled WGS sequence.
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; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF033735; G3PDH_Arsen; 1.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR42955; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42955:SF1; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 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,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184171}.
FT   DOMAIN          3..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         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         316
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   335 AA;  36645 MW;  D217738749374220 CRC64;
     MSIKVGINGF GRMGRLAVRA AWEWPEFEIV HINEIKGGAE CAAHLLEFDS VHGHWDKQIG
     FSNDALTIDG KNIGFSEHSA PGDVPWDELG VDIVIEASGK FRTTELLQPY YDRGVKKVIV
     AAPVKQGALN IVMGVNDHLY DPAEHHLLTA ASCTTNCLAP VVKVLHEKIG IEHGVITTIH
     DATNTQVVID APHKDLRRAR AASMSLIPTT TGSATAITLI YPELKGKLNG HAIRVPLLTG
     SITDAVFEMK REITAEEVNQ LFHEAAQGEL KGILGIEDRP LVSIDFKSDT RSGIVDGPST
     MVVDGNQLKV FIWYDNEMGY AHRMMELCRK VAVSL
//
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