ID A0A087SBQ6_AUXPR Unreviewed; 688 AA.
AC A0A087SBQ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic {ECO:0000313|EMBL:KFM23160.1};
GN ORFNames=F751_3351 {ECO:0000313|EMBL:KFM23160.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM23160.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM23160.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM23160.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KL662089; KFM23160.1; -; Genomic_DNA.
DR RefSeq; XP_011396030.1; XM_011397728.1.
DR AlphaFoldDB; A0A087SBQ6; -.
DR SMR; A0A087SBQ6; -.
DR STRING; 3075.A0A087SBQ6; -.
DR GeneID; 23614742; -.
DR KEGG; apro:F751_3351; -.
DR eggNOG; KOG0657; Eukaryota.
DR eggNOG; KOG1153; Eukaryota.
DR OrthoDB; 275384at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 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 InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
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 Pfam; PF00082; Peptidase_S8; 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 SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS00071; GAPDH; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT DOMAIN 358..507
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 688 AA; 70325 MW; A857B33AE87B0C32 CRC64;
MPSAMPSGSS SSPSVVEVQA SSLQSGQPPP PPTPSGTDRW ILQWRNASSE AAAAACAASD
CGLRFSRSVG GDADQLAAGA ESRAGRWGLD RVDQSALPLD GLYHYADDAA TVTVYVVDTG
ILASHEEFRS SSGNSTSRAA EAYTTLSSGT PGSDCQGHGT HVAGVVGGLS YGVAKGVALR
AVRMLDCQGQ GLVSDAVAAL DWLADNAARP AVVTLSLSGV ESVALDQAVA AAVAAGLHVV
AAAGNGDVDA CSVSPGRATA ALIVGASDER DRRLYAGDGV ASNYGACVDL FAPGSNIQSA
GITSDTASAY RSGTSQAVPF VAGAAALVLQ DQPSLAPAAV ASLLRDGATT GISTMAKVKL
GINGFGRIGR LVARAALQSD KVEIVAYNDP FIHGEYAAYM LKYDSVHGVL EGDIVGSEDG
ISVNGKMIRG FDKMKAEEIP WGEAGVDIVC ESTGVFTDVA KAGAHLKGGA KRVVISAPSP
DAPMYVMGVN HTEFDAANDT VVSNASCTTN CLAPLAKVIH DKFGIKEGLM TTVHATTATQ
KTVDGPSKKD WRGGRAVGNN IIPSSTGAAK AVGKVLPALN GKLTGMAFRV PTLDVSVVDL
TVVLEKPAKY ADILAALKAA SEGELKGILG YTEDAVVSSD FIGNPLSSIV DAQAGIQLND
TFVKIVSWYD NEWGYSNRLV DLVAHIGA
//
