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Database: UniProt
Entry: D2B7Z8_STRRD
LinkDB: D2B7Z8_STRRD
Original site: D2B7Z8_STRRD 
ID   D2B7Z8_STRRD            Unreviewed;       291 AA.
AC   D2B7Z8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=NAD_Gly3P_dh, NAD-dependent glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ACZ83929.1};
GN   OrderedLocusNames=Sros_0924 {ECO:0000313|EMBL:ACZ83929.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ83929.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ83929.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
RN   [2] {ECO:0007829|PDB:5OCM}
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX   PubMed=29733377; DOI=10.1093/protein/gzy006;
RA   Lenz M., Fademrecht S., Sharma M., Pleiss J., Grogan G., Nestl B.M.;
RT   "New imine-reducing enzymes from beta-hydroxyacid dehydrogenases by single
RT   amino acid substitutions.";
RL   Protein Eng. Des. Sel. 31:109-120(2018).
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080}.
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DR   EMBL; CP001814; ACZ83929.1; -; Genomic_DNA.
DR   RefSeq; WP_012887675.1; NC_013595.1.
DR   PDB; 5OCM; X-ray; 1.81 A; A/B/C/D/E/F=1-291.
DR   PDBsum; 5OCM; -.
DR   AlphaFoldDB; D2B7Z8; -.
DR   SMR; D2B7Z8; -.
DR   STRING; 479432.Sros_0924; -.
DR   KEGG; sro:Sros_0924; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_2_1_11; -.
DR   OrthoDB; 4535742at2; -.
DR   Proteomes; UP000002029; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR048666; RedAm-like_C.
DR   PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   Pfam; PF21761; RedAm-like_C; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5OCM};
KW   Nucleotide-binding {ECO:0007829|PDB:5OCM};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   DOMAIN          6..160
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          162..287
FT                   /note="NADPH-dependent reductive aminase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21761"
FT   BINDING         11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         33
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         68
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         94
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
FT   BINDING         232
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007829|PDB:5OCM"
SQ   SEQUENCE   291 AA;  30017 MW;  4E4962F230D53806 CRC64;
     MRDTDVTVLG LGLMGQALAG AFLKDGHATT VWNRSEGKAG QLAEQGAVLA SSARDAAEAS
     PLVVVCVSDH AAVRAVLDPL GDVLAGRVLV NLTSGTSEQA RATAEWAAER GITYLDGAIM
     AIPQVVGTAD AFLLYSGPEA AYEAHEPTLR SLGAGTTYLG ADHGLSSLYD VALLGIMWGT
     LNSFLHGAAL LGTAKVEATT FAPFANRWIE AVTGFVSAYA GQVDQGAYPA LDATIDTHVA
     TVDHLIHESE AAGVNTELPR LVRTLADRAL AGGQGGLGYA AMIEQFRSPS A
//
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