6PGD_LACLA
ID 6PGD_LACLA Reviewed; 472 AA.
AC Q9CHU6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; OrderedLocusNames=LL0622; ORFNames=L0046;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC to NADPH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE005176; AAK04720.1; -; Genomic_DNA.
DR PIR; F86702; F86702.
DR RefSeq; NP_266778.1; NC_002662.1.
DR RefSeq; WP_003129534.1; NC_002662.1.
DR AlphaFoldDB; Q9CHU6; -.
DR SMR; Q9CHU6; -.
DR STRING; 272623.L0046; -.
DR PaxDb; Q9CHU6; -.
DR PRIDE; Q9CHU6; -.
DR EnsemblBacteria; AAK04720; AAK04720; L0046.
DR KEGG; lla:L0046; -.
DR PATRIC; fig|272623.7.peg.664; -.
DR eggNOG; COG0362; Bacteria.
DR HOGENOM; CLU_024540_4_2_9; -.
DR OMA; VIMVKAG; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000002196; Chromosome.
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:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
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 PANTHER; PTHR11811; PTHR11811; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW Reference proteome.
FT CHAIN 1..472
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090045"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 128..130
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 52424 MW; 6EF4F504F217E55F CRC64;
MAQANFGVVG MAVMGKNLAL NVESRGYTVA IYNRTTSKTE EVYKEHQDKN LVLTKTLEEF
VGSLEKPRRI MLMVQAGAAT DATIKSLLPL LDKGDILIDG GNTHFPDTMR RNAELADSGI
NFIGTGVSGG EKGALLGPSM MPGGQKEAYD LVAPIFEQIA AKAPQDGKPC VAYMGANGAG
HYVKMVHNGI EYGDMQLIAE SYDLLKRVLG LSNAEIQAIF EEWNEGELDS YLIEITKEVL
KRKDDEGEGY IVDKILDKAG NKGTGKWTSE SALDLGVPLP LITESVFARY ISTYKDERVK
ASKVLSGPAV NFSGDKKEVI EKIRKALYFS KIMSYAQGFA QLRKASEEFD WDLPYGTIAQ
IWRAGCIIRA EFLQNITDAF DKDSELENLL LDDYFVDITK RYQEAVRDVV SLAVQAGIPI
PTFTSAISYY DSYRSENLPA NLIQAQRDYF GAHTYERTDK AGIFHYDWYT ED
