ID A0A060UTJ9_9PROT Unreviewed; 338 AA.
AC A0A060UTJ9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase A (GAPDH-A) {ECO:0000313|EMBL:CDQ11646.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:CDQ11646.1};
DE SubName: Full=Type I glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:QQD73099.1};
GN Name=cbbG {ECO:0000313|EMBL:CDQ11646.1};
GN Synonyms=gap {ECO:0000313|EMBL:QQD73099.1};
GN ORFNames=AFERRI_560195 {ECO:0000313|EMBL:CDQ11646.1}, H2515_01805
GN {ECO:0000313|EMBL:QQD73099.1};
OS Acidithiobacillus ferrivorans.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ11646.1, ECO:0000313|Proteomes:UP000029069};
RN [1] {ECO:0000313|EMBL:CDQ11646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ11646.1};
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ11646.1, ECO:0000313|Proteomes:UP000029069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ11646.1,
RC ECO:0000313|Proteomes:UP000029069};
RA Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V.,
RA Bonnefoy V.;
RT "Initial genome analysis of the psychrotolerant acidophile
RT Acidithiobacillus ferrivorans CF27: insights into iron and sulfur oxidation
RT pathways and into biofilm formation.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QQD73099.1, ECO:0000313|Proteomes:UP000595420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJFY6S-08 {ECO:0000313|EMBL:QQD73099.1,
RC ECO:0000313|Proteomes:UP000595420};
RA Yan L., Ni Y.;
RT "Complete genome sequence analysis of Acidithiobacillus ferrivorans XJFY6S-
RT 08 reveals extreme environmental adaptation to alpine acid mine drainage.";
RL Submitted (JUL-2020) 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 ---------------------------------------------------------------------------
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; CCCS020000052; CDQ11646.1; -; Genomic_DNA.
DR EMBL; CP059488; QQD73099.1; -; Genomic_DNA.
DR RefSeq; WP_014027694.1; NZ_LVZL01000055.1.
DR OrthoDB; 5288894at2; -.
DR Proteomes; UP000029069; Unassembled WGS sequence.
DR Proteomes; UP000595420; Chromosome.
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 GO; GO:0050661; F:NADP binding; 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; 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; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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.
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:0000313|EMBL:CDQ11646.1}.
FT DOMAIN 3..156
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 155..157
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 186
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 214..215
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 237
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 183
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 338 AA; 36408 MW; 67F148E16C42C621 CRC64;
MALRIGINGY GRIGRNILRA VYEANRTDKV QIVAVNDLGS PETNAHLTQY DSVHGRFFLP
VSVDGGDMLV GDDRVKVLAE RDPAKLPWGD LGVDVVLECT GFFASREKAA LHLKGGAKKV
LISAPAKDAV DLTVVYGVNH QLLDPAKHHI VSNGSCTTNC LAPLAKTLND LAGIEGGTMN
TIHSMTNDQR IIDVYHEDLR RARAAGMSMI PTSTGAAKAI GLVLPELAGK LDGFAIRVPT
QNVSLVDLTC IVNKEVSVDE IHAAMKAASQ GALKGVYGYN DKPLVSIDFN HNPHSSTYES
SLTKVKGKLV KVCSWYDNEW GFSNRMVDTA LAMMGQAR
//
