ID A0A2N3PW95_9PROT Unreviewed; 352 AA.
AC A0A2N3PW95;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=6-phosphogluconate dehydrogenase (Decarboxylating) {ECO:0000313|EMBL:PKU24661.1};
GN Name=gnd {ECO:0000313|EMBL:PKU24661.1};
GN ORFNames=CWS72_09960 {ECO:0000313|EMBL:PKU24661.1};
OS Telmatospirillum siberiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Telmatospirillum.
OX NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU24661.1, ECO:0000313|Proteomes:UP000233293};
RN [1] {ECO:0000313|Proteomes:UP000233293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA Pester M., Loy A.;
RT "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT cycling.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000256|ARBA:ARBA00004959}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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:PKU24661.1}.
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DR EMBL; PIUM01000009; PKU24661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PW95; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000233293; Unassembled WGS sequence.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
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:UniProtKB-UniPathway.
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; 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.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Reference proteome {ECO:0000313|Proteomes:UP000233293}.
FT DOMAIN 186..329
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT REGION 322..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 37661 MW; D2C716A9BD1264EC CRC64;
MRVGVVGLGR MGGNIARRLM KAGHGCVVFD ALDEPREVLA KEGATAVLSL ADMVTTLGEN
PRVIWVMLPA GRITEATVEC LADLLGPGDI VIDGGNSHYK DDIRRAKTLA ERRISYVDCG
TSGGVWGVER GYCMMIGGLK ESVDYLDPIF SALAPGMGGI ARTPGRENGE SRAERGYIHA
GPSGAGHFVK MVHNGIEYGL MQAYAEGFDI LRNKDSANLP EDQRFALNLA DIAEVWRRGS
VISSWLLDLG AAALVADPQL SGFSGFVQDS GEGRWTIEAA MEEAVPAEVL SSALYARFRS
RQEHSFGEKM LSAMRFAFGG HIEAGGPIEP EPHPENTEGR STTQNGAGQS HA
//
