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Database: UniProt
Entry: A0A0Q5AXA8_9MICO
LinkDB: A0A0Q5AXA8_9MICO
Original site: A0A0Q5AXA8_9MICO 
ID   A0A0Q5AXA8_9MICO        Unreviewed;       493 AA.
AC   A0A0Q5AXA8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:KQQ06031.1};
DE            EC=1.2.1.12 {ECO:0000313|EMBL:KQQ06031.1};
GN   ORFNames=ASF42_05730 {ECO:0000313|EMBL:KQQ06031.1};
OS   Rathayibacter sp. Leaf294.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1736326 {ECO:0000313|EMBL:KQQ06031.1, ECO:0000313|Proteomes:UP000051858};
RN   [1] {ECO:0000313|Proteomes:UP000051858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf294 {ECO:0000313|Proteomes:UP000051858};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf294 {ECO:0000313|Proteomes:UP000051858};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQQ06031.1}.
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DR   EMBL; LMNO01000001; KQQ06031.1; -; Genomic_DNA.
DR   RefSeq; WP_056039725.1; NZ_LMNO01000001.1.
DR   AlphaFoldDB; A0A0Q5AXA8; -.
DR   Proteomes; UP000051858; Unassembled WGS sequence.
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   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,
KW   ECO:0000313|EMBL:KQQ06031.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051858}.
FT   DOMAIN          131..292
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   493 AA;  53815 MW;  3D5424431DD02BF3 CRC64;
     MMNLTDHLLR ASSWEDRQAA AEMMIPLIGE LYRRRNVITS LHGRSLINQS AVELLKAHRF
     ARHIDEVELP LAETLPIVRA LGDLDLAASS IDVGHLAYLY RSHGAGQDLA EFLRTELAPV
     VGATLPRHAP RDVVLYGFGR IGRLIARILI EHGDTASGTR LSAIVVRKGS ANDLVKRASL
     LRRDSVHGPF NGTISIDEEH DTILANGTLI QVIYSDSPAS VDYTQYGITD AIVIDNTGRW
     RDEEGLRQHL HSRGVARVLL TAPGKGELKN VVYGINHDSI TDSDRIVTAA SCTTNAITPV
     LKMIDDYCGV DSGHIETVHS FTNDQNLIDN FHAGDRRGRA ATLNMVITET GAAKAVAKAL
     PGMAGKLTGS AIRVPTPNVS LAILNLRTTR PVTREEINRH LRTASLDSPL RRQIDYLESP
     EIVSSDILGS RHAGVVDGLA TIATEDHLVL YVWYDNEVGY SCQVVRVLEE MAGGRLPAFP
     TPRHLIDATP VLA
//
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