ID A0A074KVA6_9BACT Unreviewed; 631 AA.
AC A0A074KVA6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN ORFNames=EL17_10495 {ECO:0000313|EMBL:KEO73916.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO73916.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO73916.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO73916.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KEO73916.1}.
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DR EMBL; JMIH01000018; KEO73916.1; -; Genomic_DNA.
DR RefSeq; WP_035074000.1; NZ_JMIH01000018.1.
DR AlphaFoldDB; A0A074KVA6; -.
DR STRING; 1048983.EL17_10495; -.
DR eggNOG; COG0362; Bacteria.
DR eggNOG; COG3265; Bacteria.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000027821; Unassembled WGS sequence.
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:UP000027821};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 342..627
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 631 AA; 70519 MW; 12D2904C317513D6 CRC64;
MVIIVFGVSG SGKTTTGQLL ATQLNMPFYD ADDFHPAENV KKMSAGIPLQ DEDRKHWLEE
LAENIKEWSK GKGAVLACSA LKERYRKQLN VSDNIHWVFL KGSPDLINQR INARKNHYMN
PVLLNSQIAD LEMPEYGITV DIIKAPHLIV RRIMDRLENR VFNFGVIGMG VMGRNLALNQ
AEKGTKVAIY NRHVLGSEEG IAAQVVQDNP DFHLAAFDDL KDFVTSMTSP RVILLMIPAG
RPIDMQLDDL IPLLEKGDVV IDGGNSYYKD SKLRSQRLAE HGLHFLPMGV SGGEEGARKG
PSMMPGGSKE GYDIAKPFLE PMAAVDKNLK PCITYVGPEG SGHFVKMVHN SIEYGEMQLL
AEVYYIFRKN WGMDPIEISE VFATWRDHHL DSYLLEITIN ILKKKDGEHY LLDMILDQAE
QKGTGGWSVG TALEYGVPYG PLVEAVMART LSARKQFRTE MSKLIAYKPA AGFVKDENTD
RVKNAYAMVS LLNHAIGFDL IQTVSKTNGW DINLSEVSRI WTNGCIIRST LMDDLVNIFK
ESEDVFSSLK AVEAFGESQV DLAYTVSQSL NEGTAIPVMS SALNYYLGNI TKDSPANMIQ
AQRDYFGAHT YRRVDADSST YFHTDWTADH D
//
