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Database: UniProt
Entry: A0A223CWH2_9BACL
LinkDB: A0A223CWH2_9BACL
Original site: A0A223CWH2_9BACL 
ID   A0A223CWH2_9BACL        Unreviewed;       351 AA.
AC   A0A223CWH2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Type II glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ASS73662.1};
GN   ORFNames=CIG75_00840 {ECO:0000313|EMBL:ASS73662.1};
OS   Tumebacillus algifaecis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS73662.1, ECO:0000313|Proteomes:UP000214688};
RN   [1] {ECO:0000313|EMBL:ASS73662.1, ECO:0000313|Proteomes:UP000214688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=THMBR28 {ECO:0000313|EMBL:ASS73662.1,
RC   ECO:0000313|Proteomes:UP000214688};
RX   PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA   Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT   "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL   Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
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DR   EMBL; CP022657; ASS73662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223CWH2; -.
DR   KEGG; tab:CIG75_00840; -.
DR   OrthoDB; 9779394at2; -.
DR   Proteomes; UP000214688; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0006096; P:glycolytic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01546; GAPDH-II_archae; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214688}.
FT   DOMAIN          5..143
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        143
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
SQ   SEQUENCE   351 AA;  38338 MW;  EB8220C1D4A41B49 CRC64;
     MMKSVRIGVI GCGTIGKRVA DAVRLQSDMQ LVGIGLRTPN PTALSAHLSG IPLFCTDPMR
     FDRFEKGGLP CAGGLRDLLS QVDVILDCTQ AGEGAKRLAL YQEMGVKSIF QGGEKHATTG
     LTFSTFGNFE DAIGRSAVRV GSCNTTGLVR LLSTLDRYWG VKHAEGSLVR CSTDPDKAEN
     GLPNGAAPVF GLSHHGPDAQ LVMPTLSIFT QAVAVPMFFS HVQMMSVKLN KPADRDEVMN
     VLCNTPRILV ESHRKVGKTT AQLSHYYAET PRMRGDRQEL LLWEESIVVE GDQLHAMTSI
     DMQCITIPET IDCIRAVMGL ETERNRCMWQ TDSALGIQKH EVCYQPSSLT V
//
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