ID A0A1B8J8A3_9HELI Unreviewed; 461 AA.
AC A0A1B8J8A3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding domain-containing protein {ECO:0000259|SMART:SM00846};
GN ORFNames=BA723_06585 {ECO:0000313|EMBL:OBV29161.1}, BKN38_00990
GN {ECO:0000313|EMBL:OHU85625.1};
OS Helicobacter sp. CLO-3.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=211 {ECO:0000313|EMBL:OBV29161.1, ECO:0000313|Proteomes:UP000092701};
RN [1] {ECO:0000313|EMBL:OBV29161.1, ECO:0000313|Proteomes:UP000092701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC1 {ECO:0000313|EMBL:OBV29161.1,
RC ECO:0000313|Proteomes:UP000092701};
RA Greninger A.L., Bateman A., Jerome K., Fang F.;
RT "Genome sequence of Helicobacter sp. CLO-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OHU85625.1, ECO:0000313|Proteomes:UP000179541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLO-3 {ECO:0000313|EMBL:OHU85625.1,
RC ECO:0000313|Proteomes:UP000179541};
RA Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL Submitted (OCT-2016) 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:OBV29161.1}.
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DR EMBL; MAMQ01000073; OBV29161.1; -; Genomic_DNA.
DR EMBL; MLQN01000002; OHU85625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8J8A3; -.
DR STRING; 211.BKN38_00990; -.
DR Proteomes; UP000092701; Unassembled WGS sequence.
DR Proteomes; UP000179541; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 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 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; 2.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092701}.
FT DOMAIN 1..282
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 139..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50180 MW; DF90DD9B8C7500B6 CRC64;
MKIAINGFGR LGRCIARVAL QRGDVEIVGI NDIANHENLA YLFQKDSMHG ALGRRARIEN
ECLVLESLQD DALVDFSALV DFGKANAYKS VDSGKWADFG ALAESSLQES SLEKSSLAGS
SKMRDSGANL DSARIMLESS ASQDSTTQNS TSQDSTTQDS TTPRQPAQHA PNTPNTQDLQ
RAQHTQAMQS TRQEQATQNA RISIPFFSHS DPTKLDFKAL GADVVIESSG IFLQSAQVAH
HIQKGVPRVI ISAPATDDTP TFVLGVNHCA YAGERIISNA SCTTNCLAPI AMILEREFGI
REATLSTIHS YTNDQSLLDV PHRSDKRRSR AAGINIIPTT TGAAKSLYKV IPSLKGKIHG
HSLRVPVADV SMVDLNAFLQ KSVDARTLNE LFEAESKGAL KGILGIDDEY GVSSDFLNDA
RSSIIARDLT FCLQNMCKVM SWYDNEWGYS NRILDMAKVI L
//
