ID A0A3A5MG70_9MICC Unreviewed; 499 AA.
AC A0A3A5MG70;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=D6T63_04090 {ECO:0000313|EMBL:RJT81938.1};
OS Arthrobacter cheniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1258888 {ECO:0000313|EMBL:RJT81938.1, ECO:0000313|Proteomes:UP000272560};
RN [1] {ECO:0000313|EMBL:RJT81938.1, ECO:0000313|Proteomes:UP000272560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hz2 {ECO:0000313|EMBL:RJT81938.1,
RC ECO:0000313|Proteomes:UP000272560};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Arthrobacter.";
RL Submitted (SEP-2018) 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}.
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:RJT81938.1}.
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DR EMBL; QZVT01000002; RJT81938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5MG70; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000272560; 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}.
FT DOMAIN 138..299
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 499 AA; 54551 MW; 490DD0FFC919862E CRC64;
MQHWTENRDT WLEREALAEA MIPLIGRLYR RNNVVTSIHG RSLINKSTMN ILKAHRFARR
ITTEELRVED TAPLLEILAN LDLGAAAIDL GRLRLAYDRA RTTTDHGHAD DGPSLEDFVR
AELADIIGQG GRDERTTTDV VLYGFGRIGR LVARLLLEKS GGGHGLRLRA VVVRRGSDND
LTKRASLLRR DSVHGSFEGT IQVDEATDTI TANGVRIQVI YSDDPSSIDY TAYGISDAII
VDNTGRWRDE EGLSQHLAST GVAKVLLTAP GKGTLKNIVH GINHATIDDD DRIITAASCT
TNAITPVLKA INDRYGVIHG HVETVHSFTN DQNLIDNFHK GDRRGRSAAL NMVLTETGAA
TAVAKALPEL AGKLTGSSIR VPTPDVSIAI LNLTLQKETT KDEVNTYLRE MSLHSGMRKQ
VDYIDSPEVV STDFVGSRRA GIVDGLATIA DGTYLVLYVW YDNEFGYSCQ VVRVLEEMAG
VHPPSYPAAD LNEALAATV
//