ID D0WC15_NEILA Unreviewed; 393 AA.
AC D0WC15;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|ARBA:ARBA00018193, ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011, ECO:0000256|RuleBase:RU000485};
GN Name=gnd {ECO:0000313|EMBL:EEZ74865.1};
GN ORFNames=NEILACOT_05094 {ECO:0000313|EMBL:EEZ74865.1};
OS Neisseria lactamica ATCC 23970.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546265 {ECO:0000313|EMBL:EEZ74865.1, ECO:0000313|Proteomes:UP000003843};
RN [1] {ECO:0000313|EMBL:EEZ74865.1, ECO:0000313|Proteomes:UP000003843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23970 {ECO:0000313|EMBL:EEZ74865.1,
RC ECO:0000313|Proteomes:UP000003843};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002526}.
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 Evidence={ECO:0000256|ARBA:ARBA00000530,
CC ECO:0000256|RuleBase:RU000485};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|RuleBase:RU000485}.
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:EEZ74865.1}.
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; ACEQ02000028; EEZ74865.1; -; Genomic_DNA.
DR AlphaFoldDB; D0WC15; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000003843; 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: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; 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 NCBIfam; TIGR00873; gnd; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485}; NADP {ECO:0000256|RuleBase:RU000485};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000485,
KW ECO:0000313|EMBL:EEZ74865.1};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000485}.
FT DOMAIN 179..393
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 393 AA; 43000 MW; 5C17E8B096E17E4A CRC64;
MKGDIGVIGL AVMGQNLILN MNDCGFKVVA YNRTTAKVDE FLNGAAKGTN IIGAYSLQDL
VDKLEKPRKI MMMVRAGSVV DDFIEQLLPL LDEGDIIIDG GNANYSDSTR RTRYLTEKGI
LFVGAGVSGG EEGARRGPSI MPGGDVRAWD AVKPIFQAIA AKTPQGEPCC DWVGKDGAGH
FVKMVHNGIE YGDMQLICEA YQFMKDGLGL SYDEMHRVFA EWNKTELDSY LIEITAAILA
YKDEGGEPLV EKILDTAGQK GTGKWTGINA LDLGIPLTLI SEAVFARCVS SFKEQRVRMG
GLFARQALPV GGDKKQWVGD LRQALLASKI ISYAQGFMLI REAGESYGWD LDYGNTALLW
REGCIIRSAF LGNIRDAYEN NPDLVFLGED GYF
//