ID   A0A3M8GHG8_9FLAO        Unreviewed;       482 AA.
AC   A0A3M8GHG8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:RNC89818.1};
DE            EC=1.2.1.12 {ECO:0000313|EMBL:RNC89818.1};
GN   ORFNames=ED555_10215 {ECO:0000313|EMBL:RNC89818.1};
OS   Allomuricauda sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=192149 {ECO:0000313|EMBL:RNC89818.1, ECO:0000313|Proteomes:UP000280438};
RN   [1] {ECO:0000313|EMBL:RNC89818.1, ECO:0000313|Proteomes:UP000280438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin2 {ECO:0000313|EMBL:RNC89818.1};
RA   Zheng Q., Wang Y., Jiao N.;
RT   "Metagenomics and metaproteomics analyze the interactions between
RT   Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT   Synechococcus culture.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU000397}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNC89818.1}.
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DR   EMBL; RHLF01000002; RNC89818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8GHG8; -.
DR   Proteomes; UP000280438; Unassembled WGS sequence.
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   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   ECO:0000313|EMBL:RNC89818.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280438}.
FT   DOMAIN          130..292
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   482 AA;  53402 MW;  661FB28E2E865B50 CRC64;
     MGNNNSYEKE LAFQADRRKA TTEFIKIISD LWYDKSIEVV LFKNQVIDKN VSDIINLHEY
     AGEFVQKPIS IFDSVEILRA INDINLPPSK LDIGKLTYEY HSQISSHLNV KAFVLDKLKE
     ANASKGIKPK DVVLYGFGRI GRLLARELMA KTGKGNQLRL RAIVTRGEIT KEILEKRAAL
     LRTDSVHGQF SGTVDVDEQN KALAINGTTV FVISADKPED IDYTQYGISD CLVIDNTGAF
     RDEKALSRHL VAKGVSRVLL TAPGKGIPNI VHGVNHKEFD PDETKIYSAA SCTTNAITPI
     LKVVEDSLGI KKGHLETIHA YTNDQNLVDN MHKKYRRGRA AALNMVITET GAGQAVAKAL
     PVLDGKLTSN AIRVPVPNGS LAILNLEVKN KTSKEGVNTI LKKYALEGDL VEQIKYSLSN
     ELVSSDIVGT SAPSIYDSKA TLVSADGKNI VLYVWYDNEY GYSHQVVRLA KYIAKVRRFT
     YY
//