ID U7D621_9BACT Unreviewed; 332 AA.
AC U7D621;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=CALK_1731 {ECO:0000313|EMBL:ERP31383.1};
OS Chitinivibrio alkaliphilus ACht1.
OC Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC Chitinivibrionaceae; Chitinivibrio.
OX NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP31383.1, ECO:0000313|Proteomes:UP000017148};
RN [1] {ECO:0000313|EMBL:ERP31383.1, ECO:0000313|Proteomes:UP000017148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACht1 {ECO:0000313|EMBL:ERP31383.1,
RC ECO:0000313|Proteomes:UP000017148};
RX PubMed=24112708;
RA Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA Muyzer G., Mardanov A.V., Ravin N.V.;
RT "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT candidate phylum Termite Group 3.";
RL Environ. Microbiol. 0:0-0(2013).
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:ERP31383.1}.
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DR EMBL; ASJR01000014; ERP31383.1; -; Genomic_DNA.
DR RefSeq; WP_022637168.1; NZ_ASJR01000014.1.
DR AlphaFoldDB; U7D621; -.
DR STRING; 1313304.CALK_1731; -.
DR PATRIC; fig|1313304.3.peg.1645; -.
DR eggNOG; COG0057; Bacteria.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000017148; 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; NF033735; G3PDH_Arsen; 1.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR42955; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42955:SF1; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 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 NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160};
KW Reference proteome {ECO:0000313|Proteomes:UP000017148}.
FT DOMAIN 3..150
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 332 AA; 36224 MW; A196CA9913CEA250 CRC64;
MKKRVLINGF GRMGRLFFRA AHGDPSFEIV AINEPMGDTA GLAHLLTFDS IHGTWDVPVT
HTEKSLCIAN REILHTQEKT PAAVPLPDID IVVECSGAFR KEEELVPYFK NGADTVIVSA
PVKKGACNIV YGVNDSLYRP DKKLLTAASC TTNCLAPVVK VLQENIGIAH GSITTIHNIT
NTQRIVDAPH KDLRRARACG SSLIPTTTGS ATAITMIYPE LTGKLNGLAV RVPLLNASLT
DCVFEVERDT TAEEVNALFK EASTTTLAGI LGYEERPLVS VDYTNDTRSA IIDAQSTMVV
DKRQVKILAW YDNETGYVHR MSDLCRKVAQ AL
//
