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Database: UniProt
Entry: A0A1X1QGV4_9GAMM
LinkDB: A0A1X1QGV4_9GAMM
Original site: A0A1X1QGV4_9GAMM 
ID   A0A1X1QGV4_9GAMM        Unreviewed;       483 AA.
AC   A0A1X1QGV4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=A6F71_05450 {ECO:0000313|EMBL:ORU90412.1};
OS   Cycloclasticus sp. symbiont of Poecilosclerida sp. M.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1840537 {ECO:0000313|EMBL:ORU90412.1, ECO:0000313|Proteomes:UP000193579};
RN   [1] {ECO:0000313|EMBL:ORU90412.1, ECO:0000313|Proteomes:UP000193579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Specimen M {ECO:0000313|EMBL:ORU90412.1};
RA   Rubin Blum M., Dubilier N.;
RT   "Short-chain alkanes fuel the metabolism of mussel and sponge
RT   Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, 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:ORU90412.1}.
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DR   EMBL; LWTN01000222; ORU90412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1QGV4; -.
DR   STRING; 1840537.A6F71_05450; -.
DR   Proteomes; UP000193579; 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: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:UP000193579}.
FT   DOMAIN          132..292
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   483 AA;  53737 MW;  69ED09EBCFB6EF28 CRC64;
     MSKSQHNEYL KVWEKRQEIA EAMVPIIGKI YRSSGVVLKI YGRTLINASP ITLLKLHRYV
     RQFEKTELAI QDSFEILTAL QHMKLGPVRI DLGLLAVQYK EDERKLSIDD FLTDKLAEHI
     RDIKKQIEAE PTDVVLYGFG RIGRLLARLL IERTGSGNKM RLRAIVVRKG GDNDLQKRAS
     LLRRDSVHGS FKGTIKVDEE NNTILANGNL IQVIYASHPK EIDYTKFGIK DALIVDNTGI
     RRDEAQLSEH FLAKGAAKTL LTAPGKDVKN IVYGVNTDDI SPSDKVISAA SCTTNAITPT
     LKAINDEYGI IKGHVETVHS YTNDQNLIDN YHKGERRGRA AALNMVITET GAAKAVSKAL
     PELEGKLTGN AIRVPTPNVS MAILNLSLKK ETDKKSLNSF LREIALHSPM REQIDFTTST
     EIVSTDLVGA RKACTIDSKA TIASGDSCVL YLWYDNEFGY SCQVIRVMQK MAGLDFPSLP
     IKE
//
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