ID A0A0T5ZMM4_9CHLR Unreviewed; 299 AA.
AC A0A0T5ZMM4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Gnd, 6-phosphogluconate dehydrogenase, 6-phosphogluconate dehydrogenase {ECO:0000313|EMBL:KRT64043.1};
DE EC=1.1.1.44 {ECO:0000313|EMBL:KRT64043.1};
GN ORFNames=XU10_C0005G0067 {ECO:0000313|EMBL:KRT64043.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT64043.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT64043.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT64043.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT64043.1}.
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DR EMBL; LDXM01000005; KRT64043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZMM4; -.
DR STRING; 1640513.XU10_C0005G0067; -.
DR PATRIC; fig|1640513.3.peg.653; -.
DR Proteomes; UP000051896; Unassembled WGS sequence.
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; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Oxidoreductase {ECO:0000313|EMBL:KRT64043.1}.
FT DOMAIN 167..295
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 299 AA; 32250 MW; 6E8B1FF0605117DF CRC64;
MDLAIVGLGR MGGNMARRLQ RAGHRVVAFN RSPEKTREIM AEGLEGAFTA EEAVGMLPAP
HIVWLMVPAG DATEATLEEF AAVLSPGDWI VDGGNANFHD SKRRHGMLRE RGLRFVDAGI
SGGVWGLQNG YGTMVGGDRE DVEPLEPIFR SLAPEGGYVH CGPAGSGHYV KMVHNGIEYG
LMQAYAEGFE ILHASEYSLD LEAVAKTWQH GTVIRSWLLE LAGLAFAEHG EGLEDIKGWV
ADSGEGRWTV AEAMALDVPA PIITLSLLAR FASRQDESYG AKVLAALRQQ FGGHALKTD
//