ID Q0RVH8_RHOJR Unreviewed; 298 AA.
AC Q0RVH8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=Phosphogluconate dehydrogenase (Decarboxylating) {ECO:0000313|EMBL:ABH00708.1};
DE EC=1.1.1.44 {ECO:0000313|EMBL:ABH00708.1};
GN Name=gnd4 {ECO:0000313|EMBL:ABH00708.1};
GN OrderedLocusNames=RHA1_ro11061 {ECO:0000313|EMBL:ABH00708.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL3 {ECO:0000313|EMBL:ABH00708.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABH00708.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP000434; ABH00708.1; -; Genomic_DNA.
DR RefSeq; WP_011600336.1; NC_008271.1.
DR AlphaFoldDB; Q0RVH8; -.
DR KEGG; rha:RHA1_ro11061; -.
DR PATRIC; fig|101510.16.peg.8892; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_11; -.
DR OrthoDB; 9804542at2; -.
DR Proteomes; UP000008710; Plasmid pRHL3.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR NCBIfam; TIGR00872; gnd_rel; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF67; 6-PHOSPHOGLUCONATE DEHYDROGENASE YQEC-RELATED; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Oxidoreductase {ECO:0000313|EMBL:ABH00708.1};
KW Plasmid {ECO:0000313|EMBL:ABH00708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 162..289
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 298 AA; 32092 MW; 04B58B4A89953EDC CRC64;
MQIGLIGLGR MGGNMRERVR AAGHEVVGFD ADPSVSDVES LAELVFHLSA PRLVWVMVPA
GDPTRTVINE LSQLLAPGDL VIEGGNSRFS DDELHSDVLR EHGIGYLDCG VSGGIWGLKE
GYGLMVGGEE ADVARAMPIF DALRPPGNRD ESFVHAGPVG AGHYAKMVHN GIEYGLMQAY
AEGYELLAAE PRISAPDDVM GAWQQGTVVR SWLLELLVTA LQEDPGLSSI SGYTEDSGEG
RWTLQEAIAH AVPVPVISAA LFARFSSRQE DSPTMKAVSA LRKQFGGHQV RIMEAMQW
//
