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Database: UniProt
Entry: A0A258HDI9_9MICO
LinkDB: A0A258HDI9_9MICO
Original site: A0A258HDI9_9MICO 
ID   A0A258HDI9_9MICO        Unreviewed;       482 AA.
AC   A0A258HDI9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:OYX54382.1};
GN   ORFNames=B7Y93_06370 {ECO:0000313|EMBL:OYX54382.1};
OS   Micrococcales bacterium 32-70-13.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX   NCBI_TaxID=1970540 {ECO:0000313|EMBL:OYX54382.1, ECO:0000313|Proteomes:UP000231631};
RN   [1] {ECO:0000313|EMBL:OYX54382.1, ECO:0000313|Proteomes:UP000231631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32-70-13 {ECO:0000313|EMBL:OYX54382.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYX54382.1}.
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DR   EMBL; NCEJ01000085; OYX54382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258HDI9; -.
DR   Proteomes; UP000231631; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
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}.
FT   DOMAIN          128..289
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   482 AA;  52176 MW;  0F0C789A06569C67 CRC64;
     MTDAAVAQRE AWKARESLAE QFIPLIGRLY REHGVVTSIH GRRLINQSPI GVIKAHRYAH
     HVTGSVLPLE QTKQVLDALL TLDPGPASLD IARLLSDFER HGSGRSLTGY LGEVLAATHR
     AAPAAGGTDV VLYGFGRIGR LLARILIAHG GHGAGLHLRA IVVRRGGEND LIKRASLLRR
     DSVHGPFEGT ITVDEEASTI LANGTLIQVI YADDPASIDY TAYGIHDAIV VDNTGRWRDE
     EGLSQHLRST GVARVLLTAP GKGALPNVVH GINHESIGPE QRIVTAASCT TNAITPVLKV
     LNDEYGVVHG HVETVHSFTN DQNLIDNFHK GDRRGRSAAL NMVITETGAA KAVAKALPVL
     EGRLTGNAIR VPTPDVSMAI LNLRLERPTT RDEVNRFLRE TSLHSTLRQQ IDYIESPEVV
     STDFIGSHRA GIVDGLATIC AGENLIVYVW YDNEFGYSSQ VVRVLETMAG THPTVVPERA
     QA
//
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