ID F6CYA5_MARPP Unreviewed; 457 AA.
AC F6CYA5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN OrderedLocusNames=Mar181_0367 {ECO:0000313|EMBL:AEF53432.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF53432.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF53432.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
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; CP002771; AEF53432.1; -; Genomic_DNA.
DR RefSeq; WP_013794909.1; NC_015559.1.
DR AlphaFoldDB; F6CYA5; -.
DR STRING; 491952.Mar181_0367; -.
DR KEGG; mpc:Mar181_0367; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_1_4_6; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000009230; 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}.
FT DOMAIN 102..262
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 457 AA; 48802 MW; D7DF12B7038C1622 CRC64;
MTSTWLQSLS QVESMIPLLG KLGREKSIKV QLAGNTLMAD SVTGLMATFD QHPELDLGQV
YGVLEELYAS ELAQTCVELE DLLAQADLTS MLAAQPSDGS EVPVVLYGFG RIGRLLARRM
CALGHTTPGM KLAAIVVRNA GANDLAKRAS LLKYDSVHGA YDGIVKVDEA NQVLMINGNA
VQIIYASDPA EVDYSAYNIE KALLVDNTGR WRDHDGLSVH LNRPGIERVV LTAPGKSMKN
VVFGVNDSDL TAEDQIVSAA SCTTNAITPI LSVLEEKFGI ESGHVETVHA YTNDQNLIDN
IHKGDRRGRA AGMNMVMTET GAAKAVSKAI PSLEGKLSGS AIRVPVINVS IAVLSLNLKA
GTSVDEINAL LKAASNSAEL AGQIGFSEEA DAVSSDFIGS QQAGILDSLS TKVRGNQATL
YVWYDNEYGY SCQVVRLMEK LALGQFSKAQ LLEDQAA
//
