ID Q5QX52_IDILO Unreviewed; 481 AA.
AC Q5QX52;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=gapC {ECO:0000313|EMBL:AAV82106.1};
GN OrderedLocusNames=IL1266 {ECO:0000313|EMBL:AAV82106.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82106.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82106.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82106.1; -; Genomic_DNA.
DR RefSeq; WP_011234512.1; NC_006512.1.
DR AlphaFoldDB; Q5QX52; -.
DR STRING; 283942.IL1266; -.
DR KEGG; ilo:IL1266; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_1_1_6; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000001171; Chromosome.
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: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:UP000001171}.
FT DOMAIN 131..292
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 481 AA; 53190 MW; 79FDCD44A31D21D2 CRC64;
MNSNQQDPTL SSWQERQEFA EQMQPLLGKL YRNFGVEILV YGRSLLNVST INIIKAHRLI
LRHEGQKVRL RESFPFLQAM AELKLSPARV DLGKLAYGYL FGDKADGLSV TDYVKRELAD
IIDSEDNIEP RDVVLYGFGR IGRLLARQLI ERNGGNNKMR LRAIVVRGGR DGDLEKRASL
LRRDSIHGLF NGSITVDHDS QSIKANGTSI KVIYSNGPDQ VDYTQYGINN AIVIDNTGIW
KDEDGLGLHL KSKGVDKVLL TAPSKGDIKN IVFGVNDKMI EDSDKIVSAA SCTTNAITPV
LKAINDEFGI RNGHVETVHS YTNDQNLIDN YHTAERRGRS APLNMVITST GAAKAVAKAL
PEMAGKLTGN AIRVPTPNVS MAIMNLNFEK STSRDELNDY LRQVSLHSEL ANQIDYTAST
EIVSSDLVGS RHAGVVDSQA TIVEDDRAVL YVWYDNEFGY SCQVIRVAEA MAGLKVPNLP
K
//
