ID A0A2P6VPQ0_9CHLO Unreviewed; 2092 AA.
AC A0A2P6VPQ0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-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 Name=g431 {ECO:0000313|EMBL:PSC76060.1};
GN ORFNames=C2E20_0431 {ECO:0000313|EMBL:PSC76060.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC76060.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC76060.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC76060.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|RuleBase:RU000485}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, 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:PSC76060.1}.
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DR EMBL; LHPF02000001; PSC76060.1; -; Genomic_DNA.
DR STRING; 554055.A0A2P6VPQ0; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid 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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
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; IPR027073; 5_3_exoribonuclease.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR047007; XRN1_D1_sf.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR047008; XRN1_SH3_sf.
DR NCBIfam; TIGR00873; gnd; 1.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 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.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|RuleBase:RU000485};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649}.
FT DOMAIN 186..488
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2092 AA; 226722 MW; A7421F75195AB715 CRC64;
MSAETTKSVI GLIGLAVMGQ NLALNVAEKG FPISVYNRSG DKTDAAVARA AKEGVGERLH
GYKDLKDFVA SLERPRRIII LVKAGAPVDA TVAQLAELLE PGDIIIDGGN EWYENTERRQ
ALMKERGIFH IGMGVSGGEE GARNGPAMMP GGDAEAYKFL QPIVEKVAAQ TDDGACVTYI
GKGGSGNFVK MVHNGIEYGD MQLIAEAYDV LRVVGGLSNE ELAQVFDEWN KSELESFLVE
ITASIFKKKD EMGEGFLIDK VQDKTGMKGT GKWTIQQAAE LSVAAPTMEA ALDARFLSGL
KDERVAAEAV YASVGVQPPA AGAAAVDKQQ LIADVRAALY ASKVCSYAQG YNIIRSKSQE
QAWDIDLGSL ARIWKGGCII RAGFLDCIKQ AYLRDPALPN LLVDPDFAKD LGERQAAWRR
VVQLAVGAGI AVPGITSSLS YFDTYRRGRL PANLVQAQRD FFGSHTYERT DGKEGWFHTG
IPKFYRWLSE RYPLVNQPGG ATVVPIIDNL YLDMNGIIHN CTHGNNPEVT LSEDEMIMKI
FTYLDKLFHI VKPQKLLFMA IDGSAPRAKM NQQRARRFKS AFMGRLAAHI RFFVRKKIAE
DPAWQKPTII FSGHDVPGEG EHKIMEYIRW QKRRPNYQPN TRHCLYGLDA DLIMLSLVTH
EPHFCLLREV VSFTGGGRGQ PAREVLDNPC QEHFVLLQIG LLRDYFDAEF KPALAGRLPF
AYDLERIVDD FVLFCMLVGN DFLPPLPTVD INEGSLDAMF ALYKQMLPAL GGYLTHAGEL
SRTRLEAFMA ALAEAEADVL QARAEDAESF ESKRSRKRGG DEPAWASARV DAKRSAQEQA
RLQSEIDEDD AFALDMAKLA LQAEGDELEL LAAVEGEGEE DGEEGALPKH AITSEPTMMS
QEARNLFLNG DKDSGLAACK RRYYREKMQV SGEAARRAVV ESYIQGLHWV LEYYYRGVAS
WNWYYPFHYA PMASDLVRLP EINVSFSLGQ PFLPYEQLLA VQPSSSHRLL PAPYQPLMCD
SSSPIIDFYP TDFQIDMEGK RADWEGVVMI PFIDQDRLLA AARSVPPGSL TEEERQRNTL
GDIIVFSHAP GGAGETTYCQ TTLPAHFASV TSSNSRAVSQ AAPPPLPSGD RGFVPSFVQG
TKTGASGPAG FPSLATIKST SELRKAGVNV FGMASRKESV ILHVKGLASQ LGGQQLGAEQ
VAGALLGQRC WVKWPYLQEA VVEGVSDATV KVTRSGGTAR HGSAEASEWQ QDRQRLHQEY
LNKQGVECQD ITLLVHVRPC EGLVRQVDGT IEKRFAKKEV LYPLELVVRR NPAPDPRFQP
ETAAASLAGY DFKPGARALF LGRSYYGCMA TILPDASAGL TKKGQQLVAG QPQKKSAFRV
SLEPGPANAA TIAQSAKRVL GNINVQYTPS GQVARRLGVS NRTLGRMTGN VWLQAGEERR
DRVDVGLCVK NGAKGLYVPD FARPFMEGGE AKGWAYSEQL VRVLDDYRRR FSWLWAAIEQ
DSTPGELHLG DMLPELPREQ QVEQLGALTA WLKLNAKVAP EPAVKMLQAA LPPRAREQPA
VELENVAATL LLPPTEKGGM AAALAGGIFD IGDRVAAITG IGAPAFGARG TVVGTYDDAV
EVVFDSDVAG GSDLYGRCNG ACGMLLIASD LLNLSKPAAV KAEGEHAPRV VRTARQEAPA
AGGAASASPA VITVSRAARL NPAAALQAAT AGLTCVQPPP RPPAQPGAAV PWARVANGGG
AAAAASDKPA TKQPKLPDQH AKGFGMGRGS KAVLPPGLQL SAAAKQLPSA PGLDMPPLDV
RAPTYNGAWA ASTTGVFVDL MMHSTDFEPQ QRCKGCTSAA WGFAPREAVK LRLDGYPSAF
NSTSDFCVVA KIGAGAAFYP AGQYVLLYDG NGTVVASGDA STTGAAPGRQ LLTVTPSSGM
ELFQPSFLER VTGFTPLRFT SWQRVYGDEN NRATLPRSWT NRTTLETQTQ AGREGAFYPW
PAAAGGFVRQ PDGVAVELMV ALCNRVGADV WFSMPRADGD SDAYIAGFAA YVALNLGAAQ
KVYVEFGQNA PGWMALTQAM QTIRIGRIWR RVFSEQGQDP KRVVAVAMTD SH
//
