ID C5I4V7_9LECA Unreviewed; 277 AA.
AC C5I4V7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 2.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) {ECO:0000256|ARBA:ARBA00013119};
DE EC=1.2.1.12 {ECO:0000256|ARBA:ARBA00013119};
DE Flags: Fragment;
GN Name=GAPDH {ECO:0000313|EMBL:ACS28576.2};
OS Bryoria fremontii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae;
OC Bryoria.
OX NCBI_TaxID=283295 {ECO:0000313|EMBL:ACS28576.2};
RN [1] {ECO:0000313|EMBL:ACS28576.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S214 {ECO:0000313|EMBL:ACS28576.2};
RA Velmala S., Myllys L., Halonen P., Goward T., Ahti T.;
RT "Molecular data show that Bryoria fremontii and Bryoria tortuosa
RT (Parmeliaceae) are conspecific.";
RL Lichenologist 41:231-242(2009).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ668419; ACS28576.2; -; Genomic_DNA.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..130
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACS28576.2"
FT NON_TER 277
FT /evidence="ECO:0000313|EMBL:ACS28576.2"
SQ SEQUENCE 277 AA; 29766 MW; A450BD0777B7DFF9 CRC64;
VEHGDVKVVA VNDPFIEPHY AAYMLKYDSQ HGQFKGTIEV KGSDLVVNGQ TXKXXXEKDP
ANIPWKDTGA YYIVESTGVF TTTEKAKAHL KGGAKKVVIS APSADAAMFV MGVNEKEYKS
DIEIISNASC TTNCLAPLAK VMHDNYTIIE GLMTTIHSYT ATQKTVDGPS SKDWRGGRTA
AQNIIPSSTG AAKAVGKVIP SLNGKLTGMS MRVPTSNVSV VDLTCRLEKS VTYDQIKETM
KKASEGELKG IMSYSEDALV STDLNGDIHS CIFDATA
//
