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Database: UniProt
Entry: A0A3A5MG70_9MICC
LinkDB: A0A3A5MG70_9MICC
Original site: A0A3A5MG70_9MICC 
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
//
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