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Database: UniProt
Entry: A0A0Q5Z3L2_9BRAD
LinkDB: A0A0Q5Z3L2_9BRAD
Original site: A0A0Q5Z3L2_9BRAD 
ID   A0A0Q5Z3L2_9BRAD        Unreviewed;       300 AA.
AC   A0A0Q5Z3L2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQT08168.1};
GN   ORFNames=ASG57_08245 {ECO:0000313|EMBL:KQT08168.1};
OS   Bradyrhizobium sp. Leaf396.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT08168.1, ECO:0000313|Proteomes:UP000051536};
RN   [1] {ECO:0000313|EMBL:KQT08168.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT08168.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT08168.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT08168.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQT08168.1}.
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DR   EMBL; LMQJ01000045; KQT08168.1; -; Genomic_DNA.
DR   RefSeq; WP_057198505.1; NZ_LMQJ01000045.1.
DR   AlphaFoldDB; A0A0Q5Z3L2; -.
DR   OrthoDB; 9812907at2; -.
DR   Proteomes; UP000051536; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          7..166
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          173..288
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   300 AA;  30901 MW;  BD5525E0029F74AA CRC64;
     MTDALGNVAF IGIGKMGLPM SVLVAKAGFA VTAFDQSAVR INEARAQGIA VAASPAEAVR
     GKAAVVTSLP DDAALRGALL GPTGLIAAMT PGAVLIETST VSVEASAEIA AAAQSRGIAY
     LRSPVSGNAS IVHTGALTCF VSGPKEAFEG AKPLFAAFTR AQTYLGPAEE ARYAKLSVNL
     MIAVSAAMMA ESLALARKGG IAWQDILKVL DDSAVASPMV KYKTAPLRTR DFESTFSCRQ
     MAKDLDLILG AGHAVGVPLQ LAAQVRETYG ALVAQGDGET DFIATVKHLE RLSGLDEPKL
//
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