ID M7N7M3_9BACT Unreviewed; 762 AA.
AC M7N7M3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN Name=yqjI {ECO:0000313|EMBL:EMR04608.1};
GN ORFNames=ADICEAN_00210 {ECO:0000313|EMBL:EMR04608.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR04608.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR04608.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR04608.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(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:EMR04608.1}.
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DR EMBL; AODQ01000003; EMR04608.1; -; Genomic_DNA.
DR AlphaFoldDB; M7N7M3; -.
DR STRING; 1279009.ADICEAN_00210; -.
DR PATRIC; fig|1279009.4.peg.214; -.
DR eggNOG; COG0362; Bacteria.
DR eggNOG; COG3265; Bacteria.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000011910; 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:EMR04608.1};
KW Pentose shunt {ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000011910};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 474..760
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 762 AA; 84470 MW; 614F23FB3EAEF61C CRC64;
MQNGVILLHP LVVALGNNHA PLHQHRTNGN TPFGAALFGL CNGQFHKVIH TFCFFSFILW
PCRSQNFSTR LHCFCSNRGK ATASKHAGLR DVTAIFWAKT AEAPKPSAAF QAFRYIEEAD
PTLLLFRMIC IIMGVSGSGK TTIGQLLAQR LGLPFHDADD FHPPANIRKM QQGQPLTDLD
RKDWLEQLAA HIKQWEAGGG AVLACSALKE QYRITLQSIP RTQLRWVFLE GSRALIQQRL
KNRTGHFMSP ELLDSQLATL EKPDYGIHLN IALSPQELVE QVVTNLNAMN TLSEFGIIGL
GVMGKSLALN LAEKGVRLAL YNRHVTGTEE QVARRILEEH PHIPGMQGFD DLAAFVASLE
RPRKILLMIV AGPVVDLQIE ALLPLLDAED VLIDGGNSFY KDTARRTRLL AEKGIEFVGT
GISGGEEGAR KGPSMMPGGA QKGYQLVQHY LELMAAKDRR GLPCTAYIGP EGAGHFIKMV
HNSIEYAEMQ ALAECYQLMR EYLRLAPPAI ADTFAAWQQE ELNSYLLGIT VDIMRKQEGG
GLLLDKILDQ AEQKGTGGWS VSAALEHGVP YGPLTEAVMA RAISSRKAQR VKAATLYQHT
PARHSGNAQE FLGQLRGAYQ ACRILNHHIG FALMRAVSER EGWQLNFSEI ARIWTNGCII
RSELMEELVE LYKTEEELLL APSIIRRMKG FAPGFARIVA ESVGAGIALP VFTSALNYYL
GYQTAQSPAN LIQAQRDYFG AHTYRRVDRA ADEYFHTEWG QP
//
