ID A0A0R0LUR2_9MICR Unreviewed; 498 AA.
AC A0A0R0LUR2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) {ECO:0000256|ARBA:ARBA00013011};
DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011};
GN ORFNames=M153_15140001179 {ECO:0000313|EMBL:KRH93110.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH93110.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH93110.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH93110.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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:KRH93110.1}.
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DR EMBL; LGUB01000488; KRH93110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0LUR2; -.
DR VEuPathDB; MicrosporidiaDB:M153_15140001179; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000051530; 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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 2.
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 Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW Reference proteome {ECO:0000313|Proteomes:UP000051530}.
FT DOMAIN 209..493
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 498 AA; 56898 MW; BA16679ED6CD846C CRC64;
MPLKMTPELS KNKMHVGVLG LAAMGNNLCF NLVSNGYTVS IYNRTPDRTE KIRNEYDQYG
KYPGKFVYCY SLEEFIQSIP EPRPIFLIVM STAVRSVIES ILPLISEKDM ICDFANSVPE
HTNEHAKLIS DFFFPCNSKN EKLNCQHSDQ GNVHKARFLG IGISGGTTGA RKNGGLMISG
HLETYEHLKH VFNSLTNSSA YFGQDYATGH FIKFLHNGVE YALMSIISEF NEISCSIEKH
YDVKKENSNT SVILEEINQK LDTYLLTILK KVTSNPNFKN IDNDLRMKGS GQWVYNTFGG
RVNIGLIGNA VEQRVRKYFD NSVANSNDQI IKSQMLNDML KDKNLVQMKS ILKNALLYSL
RQCYQQGIDM ILHDNIIVKS EDKNFLIIKS LDVWRNGCII SGHIVDIVKD SYLLKNNLIK
NTELEEYFKI DESTIHENLK FLTEYALENL IPVQQIPTIL NGLNYKNDNQ IRILSGMRDY
FGAHGVYING KWQNIDWE
//
