ID A0A142EI18_9BACT Unreviewed; 631 AA.
AC A0A142EI18;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN ORFNames=AO498_00100 {ECO:0000313|EMBL:AMQ54773.1};
OS Algoriphagus sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ54773.1, ECO:0000313|Proteomes:UP000073816};
RN [1] {ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA Shintani M.;
RT "Complete sequence of Algoriphagus sp. M8-2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMQ54773.1, ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|EMBL:AMQ54773.1,
RC ECO:0000313|Proteomes:UP000073816};
RX PubMed=27174266;
RA Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA Shintani M.;
RT "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT Brackish Lake.";
RL Genome Announc. 4:0-0(2016).
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|RuleBase:RU000485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12; Evidence={ECO:0000256|ARBA:ARBA00001329};
CC -!- PATHWAY: Carbohydrate acid metabolism. {ECO:0000256|ARBA:ARBA00004761}.
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|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 -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC {ECO:0000256|ARBA:ARBA00008420}.
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DR EMBL; CP012836; AMQ54773.1; -; Genomic_DNA.
DR RefSeq; WP_067541992.1; NZ_CP012836.1.
DR AlphaFoldDB; A0A142EI18; -.
DR STRING; 1727163.AO498_00100; -.
DR KEGG; alm:AO498_00100; -.
DR PATRIC; fig|1727163.4.peg.22; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000073816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02021; GntK; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR006183; Pgluconate_DH.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR006001; Therm_gnt_kin.
DR NCBIfam; TIGR00873; gnd; 1.
DR NCBIfam; TIGR01313; therm_gnt_kin; 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 Pfam; PF01202; SKI; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW NADP {ECO:0000256|RuleBase:RU000485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000073816};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..631
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 631 AA; 69607 MW; 8871C03633EB08D5 CRC64;
MLVIVTGVSG TGKTTLGTLL SERLKLPFFD ADHFHPEENI AKMSAGHPLN DEDRQPWLQA
LADQLLSSEQ KGGAVLACSA LKNTYREKLS VTSNLRWIHL TGDRDLIWER MLARKNHYMK
AGMLDSQMAV WEKPDSGLLL DITGTPEDLL EASLHYLKSQ PMNMKMGVIG MGVMGKSLAL
NLAEKGVPVS LYNRFVAGKE EGIAQKVLDE HPEFSNMLAF EDLQQFVDSL EKPRRILMMI
PAGAAIDAQL DALLPILEKD DLVIDGGNSF YKDSERRVDR LKEVGMHFLP MGVSGGEEGA
RKGPSIMPGG NAEGYAMVED FLGRISAKDK DGKPCVTYVG PGGSGHFIKM VHNSIEYGEM
QVLAELVHVL RFGFGCSADQ VSGIFSEWGQ GELKSFLLEI TADLLLYKEI GELLLDKILD
QAGQKGTGAW SLTTALEYGI PYSPLAESVN ARGVSGEKAQ RVAFSKTFHH EFQKVDGSLE
SWLPKIKSAY ALARIINHEV GFRLMKTVSD TKDWKLNFNE ISRIWTNGCI IRSGLMENIS
ANYSDSSSFF EMPGVKEQVI SGRKDLAELV GLGLTHGFAL PVMSAGINYL LGRITAESSA
SVIQAQRDYF GAHTYQRKDD PSGKFYHTQW I
//
