ID A0A0P7GBJ4_9MICC Unreviewed; 488 AA.
AC A0A0P7GBJ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=AO716_11065 {ECO:0000313|EMBL:KPN18371.1};
OS Arthrobacter sp. Edens01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN18371.1, ECO:0000313|Proteomes:UP000054460};
RN [1] {ECO:0000313|EMBL:KPN18371.1, ECO:0000313|Proteomes:UP000054460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edens01 {ECO:0000313|EMBL:KPN18371.1,
RC ECO:0000313|Proteomes:UP000054460};
RA Couger M.B.;
RT "Draft Genome of Arthrobacter sp. strain Edens01.";
RL Submitted (SEP-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}.
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:KPN18371.1}.
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DR EMBL; LKIU01000005; KPN18371.1; -; Genomic_DNA.
DR RefSeq; WP_055240847.1; NZ_LKIU01000005.1.
DR AlphaFoldDB; A0A0P7GBJ4; -.
DR STRING; 1732020.AO716_11065; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000054460; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UP000054460}.
FT DOMAIN 130..291
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 488 AA; 53156 MW; 28C9292408B17470 CRC64;
MSQKSDTCLD AWMDREAMAE AMIPLIGRLY RENSVVTSVH GRPLVNRSVI DILKAHRFAR
QIDDVELPVA ETLPILQALT ELELGAASVD VARMNAKYQR EGNGAPLVDF LRAELADVAG
KHGADERTST DVVLYGFGRI GRLLARILID HEGGGHGLRL RAIVVRKGAE NDLVKRASLL
RRDSVHGAFP GTITVDEENN TILANGTLIQ VIYSNDPSTV DYTAYGIHDA IVVDNTGRWR
DKDGLAQHLQ AKGASRVLLT APGKGDLKNI VHGINHQAIT DEDKILSAAS CTTNAITPVL
KVLNDKFGIV NGHVETVHSF TNDQNLIDNF HKGDRRGRSA ALNMVITETG AAKAVAKALP
ELAGKLSGNA IRVPTPDVSM AILNVNLETE TTKEELNTFL RETSLNSELH KQIDYIDSPE
VVSTDFVGSK RAGIVDGLAT ISNGRNAILY VWYDNEYGYS CQVIRVLEEM AHVNPPAFPR
AEELVASL
//