ID A0A0K2YEL7_9NOCA Unreviewed; 486 AA.
AC A0A0K2YEL7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022, ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=RHCRD62_20407 {ECO:0000313|EMBL:CRK50968.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK50968.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK50968.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK50968.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-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; CVQP01000005; CRK50968.1; -; Genomic_DNA.
DR RefSeq; WP_050064230.1; NZ_CVQP01000005.1.
DR AlphaFoldDB; A0A0K2YEL7; -.
DR STRING; 260936.RHCRD62_20407; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000044872; Unassembled WGS sequence.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProt.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; 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; TIGR01534; GAPDH-I; 1.
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 ECO:0000256|RuleBase:RU361160};
KW Reference proteome {ECO:0000313|Proteomes:UP000044872}.
FT DOMAIN 127..287
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 486 AA; 52887 MW; 3BC272DF542B8D4C CRC64;
MSTAELTQWN SEEALAEAMI PIIGGLHRTH SVTVLLHSRS LVNRSVIQIL RTHRFARQIR
GDELSVEETF PFLQALTELD LRPSKIDLGL LVSAYHAHGE GTSIPEFVAE RLADLVGGAQ
TSPAKPQDVV LYGFGRIGRL VARLLIEKAG SGNGLNLRAV VVRKGGDDDL VKRASLLRRD
SVHGQFNGTI KVDAENSTLI ANGNVIKFIY SNDPTTVDYT EYGIDNAILV DNTGIWRDRD
GLSKHLRPGI AKVLLTAPGK GDVPNIVHGV NHRSLDQDEK IVSCASCTTN AIVPPLKTMD
DEFGVSRGHV ETVHSFTNDQ NLLDNYHKAD RRGRSAPFNL VLTETGAASA VAKALPDLKA
KITGNSIRVP TPDVSVAILH LHLNRETTKS EVVEHLRQES LTGELSRNLD FTAATDAVSS
DFIGSRAACI VDANATIVEG DTAILYVWYD NEFGYSCQVV RTVQYLSGVE YPIYPMVEAA
DLAAVN
//