ID   A0A1A9EWZ3_9GAMM        Unreviewed;       479 AA.
AC   A0A1A9EWZ3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ANG62436.1};
GN   ORFNames=A8C75_08005 {ECO:0000313|EMBL:ANG62436.1};
OS   Marinobacterium aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG62436.1, ECO:0000313|Proteomes:UP000078070};
RN   [1] {ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA   Baek K., Yang S.-J.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANG62436.1, ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|EMBL:ANG62436.1,
RC   ECO:0000313|Proteomes:UP000078070};
RX   PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA   Bae S.S., Jung J., Chung D., Baek K.;
RT   "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT   isolated from estuary sediment.";
RL   Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {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; CP015839; ANG62436.1; -; Genomic_DNA.
DR   RefSeq; WP_067380455.1; NZ_CP015839.1.
DR   AlphaFoldDB; A0A1A9EWZ3; -.
DR   STRING; 1821621.A8C75_08005; -.
DR   KEGG; mars:A8C75_08005; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000078070; Chromosome.
DR   GO; GO:0051287; F:NAD 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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000078070}.
FT   DOMAIN          126..287
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   479 AA;  52747 MW;  27010DE829CDC27C CRC64;
     MSQELVFADW KAREALAEAM VPLIGRLYRD RNVETSVFGR LVHKRSVTDI LKAHRFARQM
     MQDQEELSVH DTYPVLEAVD KLGVANAHVD VGKLVIKFRH EGNGDIEAFL KKELDSVIGA
     PEREPTDVVL YGFGRIGRLL ARLLIERTGG GQSLRLRAIV VRRGNAENDL EKRASLLRRD
     SVHGSFKGTI QVDEENQALI ANGNMIKVIF ADAPDTIDYT DYGISNALLI DNTGKWRDAD
     GLSLHLRATG VSRVLLTAPG KGIKNIVMGV NHQDIIDEDR ILSAASCTTN AIVPVLKKID
     EQFGVLNGHV ETVHSYTNDQ NLIDNYHKGD RRGRAAGLNM VISETGAAKA VAKALPQLEG
     KLTGNAIRVP TPNVSMAILN LNLEKETSKE ELNAYLRDAA LFSELQKQID FSTSPEAVST
     DFVGSRAAGV VDGLATIVDG KRCVLYVWYD NEFGYSCQVF RMMQAMAHCT LPAFPLKGI
//