ID A0A0M2VNI4_9GAMM Unreviewed; 484 AA.
AC A0A0M2VNI4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=VT06_01045 {ECO:0000313|EMBL:KKO50593.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO50593.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO50593.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO50593.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) 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:KKO50593.1}.
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DR EMBL; LAHP01000001; KKO50593.1; -; Genomic_DNA.
DR RefSeq; WP_046552391.1; NZ_LAHP01000001.1.
DR AlphaFoldDB; A0A0M2VNI4; -.
DR STRING; 1632859.VT06_01045; -.
DR PATRIC; fig|1632859.4.peg.205; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000034895; 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:UP000034895}.
FT DOMAIN 131..292
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 484 AA; 53621 MW; E23CBDEA36B3FA65 CRC64;
MTLSHAEQYQ KSWQERQEYA ENMQPIIGRL YRNKGIEVVV YGRPLVNATT IDIIKAHKSV
ERFEGQKLRL RECFPVLEAI SKMNLAPGRV DIGKLAYSFI FKNSGAGLTL EQYLARALVD
ILDHEDQVKP VDVVLYGFGR IGRLLARLML ERSGPSSKLR LKAIVVRGGK KGDLEKRASL
LRRDSIHGPF NGSITVDEEN QGIKANGTFI KVIYASSPEQ VDYTAYGIDN ALVVDNTGIW
KDDNELAIHF KSKGTAKVLL TAPAKGDVPN IVYGVNQHMI LPEHKFVSAA SCTTNAITPV
LKALNDEFGI RNGHVETVHS YTNDQNLIDN FHNAERRGRA APLNMVITST GAASAVAKAL
PELKGKLTGN AIRVPTPNVS MAILSLNLNK ETNREEMNAY LQRISLFSEL QDQIDFTSST
EIVSSDLVGS RYAGVVDSQA TIVDGDRCVL YVWYDNEFGY STQVIRVMND MAGIKYPTLP
VAKY
//