ID S7VKI7_9FLAO Unreviewed; 627 AA.
AC S7VKI7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN ORFNames=ADIWIN_3900 {ECO:0000313|EMBL:EPR70037.1};
OS Winogradskyella psychrotolerans RS-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR70037.1, ECO:0000313|Proteomes:UP000014962};
RN [1] {ECO:0000313|EMBL:EPR70037.1, ECO:0000313|Proteomes:UP000014962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR70037.1,
RC ECO:0000313|Proteomes:UP000014962};
RX PubMed=23950132;
RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT Ocean.";
RL Genome Announc. 1:e00630-e00613(2013).
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:EPR70037.1}.
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DR EMBL; ATMR01000206; EPR70037.1; -; Genomic_DNA.
DR RefSeq; WP_020898043.1; NZ_ATMR01000206.1.
DR AlphaFoldDB; S7VKI7; -.
DR STRING; 641526.ADIWIN_3900; -.
DR PATRIC; fig|641526.4.peg.3871; -.
DR eggNOG; COG0362; Bacteria.
DR eggNOG; COG3265; Bacteria.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000014962; 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 ECO:0000313|EMBL:EPR70037.1};
KW Pentose shunt {ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000014962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 346..627
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 627 AA; 70251 MW; 38590C5936CC19A9 CRC64;
MKQVIFVIGV SGCGKSTIGK LLAEELDLPF FDGDDFHPKA NIKKMSSGLP LNDDDRQGWL
KTLNDLAKKQ LTKNSCVIVC SALKEKYRDI LSLDIEAETK WVYLRGDFNQ IYNRVNRRRN
HFMPSELLKS QFDTLEEPKD AIQIDISLTP ESIIKTLKHK LMDKSEFGLF GLGVMGKSLC
RNLANNGFKI AMFNRHVDGV EVDIAKDFKA KFPELSQSEA FDDIAAFVNA LQQPRRIMLM
VNAGKTIDYV IEDLLPHLSE NDILIDGGNS NYVNTKERVD YLKTKGIHFI GAGVSGGEEG
ALKGPSIMPS GDLKAYKSVQ PFLEKIAAKD KNGLPCCTYV GPEGSGHFIK MVHNGVEYVE
MQLLAEVATI LEALGQIPDD IANTFETWKS TANSYLLEIT ADIFRKKEGD DWLVNKILDK
AGNKGTGNWT TMASAELGVP STLIASALFS RYISFYKEER VQLNQNFEHS RTSELNLTTN
DILEAYQFAR IINHYQGFKL ISEASNTFSW DLNLSEIARI WTNGCIIRSA LMEDLVDIFK
DTTNILTNSK LIDLVNQYRP SVKKVVSQCV LNDITTPALG EAIQFLNGIT TSYASANIIQ
AQRDYFGAHT YQRLDDDSGK NHHTNWN
//
