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Database: UniProt
Entry: A0A271IU56_9BACT
LinkDB: A0A271IU56_9BACT
Original site: A0A271IU56_9BACT 
ID   A0A271IU56_9BACT        Unreviewed;       352 AA.
AC   A0A271IU56;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:PAP74650.1};
GN   ORFNames=BSZ37_20985 {ECO:0000313|EMBL:PAP74650.1};
OS   Rubrivirga marina.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC   Rubrivirga.
OX   NCBI_TaxID=1196024 {ECO:0000313|EMBL:PAP74650.1, ECO:0000313|Proteomes:UP000216339};
RN   [1] {ECO:0000313|EMBL:PAP74650.1, ECO:0000313|Proteomes:UP000216339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAORIC-28 {ECO:0000313|EMBL:PAP74650.1,
RC   ECO:0000313|Proteomes:UP000216339};
RA   Yoshizawa S., Kumagai Y., Kogure K.;
RT   "Study of marine rhodopsin-containing bacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:PAP74650.1}.
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DR   EMBL; MQWD01000005; PAP74650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A271IU56; -.
DR   OrthoDB; 9779394at2; -.
DR   Proteomes; UP000216339; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; 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   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; 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; IPR000846; DapB_N.
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; PF01113; DapB_N; 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   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216339}.
FT   DOMAIN          7..145
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        145
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
SQ   SEQUENCE   352 AA;  37709 MW;  8592073570C79654 CRC64;
     MTHTENTRVA VNGYGVIGKR VAAAVAAQDD MTLAGVADVA TDWRVAVARA KGYPLFGATL
     EHVRAMTEAG LDPAGSLDDL LGAADVVVDC TPKKVAAGNV ERYRERGIKF IVQGGEKHAV
     TGHSFTAENN YDTALGRQST RVVSCNTTST VRTLSALKQA GLLKKARGVL IRRATDPWES
     HLGGIMNTLV PEADIPSHQG PDAQTVDPEL DVVTMAVKAP ETLSHLHYWT VQLTREASKD
     EVLGALRASS RIAFIRMADG LVALNSVKEL MADLGRPHDN LYEVAVWEDM LTVQGDEAFY
     AYMVDNQAIV IPETIDAIRA LTEIEADGAT SIEKTNEALG ITGRLVPEPV AA
//
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