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Database: UniProt
Entry: A0A1L3JMM4_9FLAO
LinkDB: A0A1L3JMM4_9FLAO
Original site: A0A1L3JMM4_9FLAO 
ID   A0A1L3JMM4_9FLAO        Unreviewed;       622 AA.
AC   A0A1L3JMM4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN   ORFNames=LPB136_03125 {ECO:0000313|EMBL:APG66388.1};
OS   Tenacibaculum todarodis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG66388.1, ECO:0000313|Proteomes:UP000181898};
RN   [1] {ECO:0000313|EMBL:APG66388.1, ECO:0000313|Proteomes:UP000181898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0136 {ECO:0000313|EMBL:APG66388.1,
RC   ECO:0000313|Proteomes:UP000181898};
RA   Kim E., Yi H.;
RT   "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; CP018155; APG66388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L3JMM4; -.
DR   STRING; 1850252.LPB136_03125; -.
DR   KEGG; ten:LPB136_03125; -.
DR   OrthoDB; 9804542at2; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000181898; 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:UP000181898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          339..620
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
SQ   SEQUENCE   622 AA;  69557 MW;  CCE78F41D8C7AB7F CRC64;
     MGVSGVGKST IGNLLSEELS IPFFDGDDFH PEENILKMSK GLALNDNDRL GWLQQLNKLA
     IEQQSKNGAI IACSALKKIY RDILYNSIKD STRFVFLDGS FNQIKERINA RKGHFMNSEL
     LKSQFDALEI PQNAIKIDIS LTPHKIVKLI SKEMDNKAEF GLFGLGVMGK SLSRNLANNG
     FKIALFNRHV KDVEVDVAKN FKNDFEELST ALPFDNIESF VGSLQKPRKI MLMVNAGKIV
     DYVIEDLLPF LEAGDVLIDG GNSNYHKTKE RFDYLKSKGI NFVGTGVSGG EEGALKGPSI
     MPGGNKATYK EVKPYLEAIA AKDANNLPCC THIGTEGSGH FVKMVHNGIE YVEMQLLAEV
     YTILKALGNN PDEIANILEG WKESTNSYLL EITIDILRKK EGEGWLVDKI MDKAGNKGTG
     NWTTITTAQL GVPSTMITSA LFARYTSFYK EERIAASKNL EVNNTLDINL TVEDVLKAYQ
     FARLINHYQG FKLIDEASKS YSWNLNLSEL ARIWTNGCII RSDLMVELVT TFKSTDNILT
     DKKVIEQLKT LKPSIKKVVS ECILNELATP NLNESISFLN SFVIENSSAN LIQAQRDYFG
     AHTYQLKNDK TNKFYHTDWT KN
//
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