ID A0A0S8D5L6_9BACT Unreviewed; 307 AA.
AC A0A0S8D5L6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE SubName: Full=6-phosphogluconate dehydrogenase {ECO:0000313|EMBL:KPK31497.1};
GN ORFNames=AMK69_00035 {ECO:0000313|EMBL:KPK31497.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK31497.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK31497.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK31497.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK31497.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJNR01000001; KPK31497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8D5L6; -.
DR PATRIC; fig|1704023.3.peg.15; -.
DR Proteomes; UP000051394; 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: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}.
FT DOMAIN 167..296
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 307 AA; 33762 MW; DBDE78B4A883C883 CRC64;
MELAIIGLGR MGMNMARRLL KGNHQVIAYN RTSNKTDEIV KQGAIGAYSL SEMVEKLSPP
RVVWLMLPAG PAIDDHLEQL KDLLSDGDVV IDGGNTYFKD DIRRAEMLAE KGIQFVDAGV
SGGIWGLKVG YCTMVGGTKA NFEYLEPIFK TLAPQDGYLY CGPTGAGHFV KMVHNGIEYG
MMQAYGEGFE ILEASPYAES LNYAEVAHLW NQGSVIRSWL LELAEEAFKK DGKLSDIRGY
VEDSGEGRWT VQQAIETAVA APVIALSLLQ RFRSRKKDTY SDKVLAALRR EFGGHAVVAS
ESKKEGD
//
