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Database: UniProt
Entry: K2BQX7_9BACT
LinkDB: K2BQX7_9BACT
Original site: K2BQX7_9BACT 
ID   K2BQX7_9BACT            Unreviewed;       295 AA.
AC   K2BQX7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 35.
DE   RecName: Full=6-phosphogluconate dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM01350};
GN   ORFNames=ACD_50C00343G0004 {ECO:0000313|EMBL:EKD64569.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD64569.1};
RN   [1] {ECO:0000313|EMBL:EKD64569.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD64569.1}.
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DR   EMBL; AMFJ01022028; EKD64569.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2BQX7; -.
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: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; IPR015815; HIBADH-related.
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   PIRSF; PIRSF000103; HIBADH; 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}.
FT   DOMAIN          160..291
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   295 AA;  32727 MW;  55C0F63C2EAF5B16 CRC64;
     MKLGFIGLGK MGSRMVTKLL DEGHEIIAWN RSAHKLKNVE TIEELVKSID KPRVVWVMVT
     AGETTQNILD EVLKYIEKDD IIIDGGNSFF KDTQRRYEEL KAKNIKFLGI GVSGGIIAAE
     EGYPLMVGGD KSAYEFVSPI LDSLAKPNGG HEYFGEGGAG HFVKMVHNGI EYGMMQSIGE
     GFGILEKSPY KLDLTKVSKL FQKGTIVSGF LMDRTAEVFS RDSSLSQVVG SIEATGEAEW
     TVNQAREENV PVELIEKALE FRKRSQEDVS IQESFTAKLI SSLRNAFGGH EIRKR
//
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