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Database: UniProt
Entry: A0A0R1XHP3_9LACO
LinkDB: A0A0R1XHP3_9LACO
Original site: A0A0R1XHP3_9LACO 
ID   A0A0R1XHP3_9LACO        Unreviewed;       477 AA.
AC   A0A0R1XHP3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN   ORFNames=FD32_GL000194 {ECO:0000313|EMBL:KRM26950.1};
OS   Limosilactobacillus panis DSM 6035.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM26950.1, ECO:0000313|Proteomes:UP000051412};
RN   [1] {ECO:0000313|EMBL:KRM26950.1, ECO:0000313|Proteomes:UP000051412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM26950.1,
RC   ECO:0000313|Proteomes:UP000051412};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000256|PIRNR:PIRNR000109}.
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|PIRNR:PIRNR000109,
CC         ECO:0000256|RuleBase:RU000485};
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|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
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:KRM26950.1}.
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DR   EMBL; AZGM01000070; KRM26950.1; -; Genomic_DNA.
DR   RefSeq; WP_047767720.1; NZ_LDPB01000031.1.
DR   AlphaFoldDB; A0A0R1XHP3; -.
DR   STRING; 1423782.FD32_GL000194; -.
DR   PATRIC; fig|1423782.4.peg.195; -.
DR   OrthoDB; 9804542at2; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000051412; Unassembled WGS sequence.
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   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   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; IPR006183; Pgluconate_DH.
DR   NCBIfam; TIGR00873; gnd; 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   PIRSF; PIRSF000109; 6PGD; 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   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW   ECO:0000256|RuleBase:RU000485};
KW   NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051412}.
FT   DOMAIN          181..474
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         458
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ   SEQUENCE   477 AA;  53141 MW;  938A15074100FD20 CRC64;
     MSENKAQIGV VGLAVMGKNL ALNIESRGFT VGVYNRHRNR TDEMMKDHSD KKLVPSYTIK
     DFVDSLEKPR RILLMVKAGK PTDAVIDELL PLLDKGDVLI DGGNTNFHDT MARNAKLDKS
     GINFIGMGVS GGELGALHGP ALMPGGQKEA YDLVAPILTQ IAAKAEDGKP CVTYVGPNGA
     GHYVKMVHNG IEYGDEELID ESYNIMRNVL KMPVDDIAKA FAEWNKGELS SYLVDITADI
     LTRKDDLGDD KSKPIVDMIL DRGANKGTGK WSSETALEGG APQSVITEAV YARYISMMKD
     ERVAASKVLP EETEAISIDD KKELIEKVRE ALYFGKVMSY AQGFEQMRID SERYNWNLKM
     GELAQIWRAG CIIRAQFLQN ITDAFDKNPD LKNLLLDDYF KDISKKYQKA IRDIVALAVK
     AGIPVPALSA AISYYDSYRA EVVPANLLQA QRDYFGAHTY ERVDRPGNYH YTWYKEQ
//
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