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Database: UniProt
Entry: A0A3L8RUH5_CHLGU
LinkDB: A0A3L8RUH5_CHLGU
Original site: A0A3L8RUH5_CHLGU 
ID   A0A3L8RUH5_CHLGU        Unreviewed;       790 AA.
AC   A0A3L8RUH5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=G6PE protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00015676 {ECO:0000313|EMBL:RLV87468.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV87468.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV87468.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV87468.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV87468.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC       {ECO:0000256|ARBA:ARBA00004959}.
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:RLV87468.1}.
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DR   EMBL; QUSF01000200; RLV87468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8RUH5; -.
DR   STRING; 44316.ENSEGOP00005015740; -.
DR   Ensembl; ENSEGOT00005018168; ENSEGOP00005015740; ENSEGOG00005012753.
DR   OMA; YCPQSGT; -.
DR   UniPathway; UPA00115; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd01400; 6PGL; 1.
DR   Gene3D; 3.40.50.1360; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR01198; pgl; 1.
DR   PANTHER; PTHR23429:SF7; GDH_6PGL ENDOPLASMIC BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..790
FT                   /note="G6PE protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018013391"
FT   DOMAIN          29..211
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          217..507
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   DOMAIN          559..781
FT                   /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01182"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   790 AA;  88061 MW;  78273AD626AC9A88 CRC64;
     MLGRVLCTVL FVGALPSPAG ASQGHISVVL LGANGDLAKK YLWQGLFQLY MDQVSSGHSF
     TFHGAALTAL EPGQRLMFDV LKKLSCPPDE APNRCAVLKD QFLKLSQYHQ LGTAEDYTAL
     NRDIETLLGQ EGLKEAGRIF YFSVPPFAYT EIARHVNSSC RPRAGAWLRV VLEKPFGHDL
     HSAQQLAAEL AGFFSEEEMY RVDHYLGKQA VAHILPFRDQ NRQFLGPIWN RHHVERVEVV
     LKETVDAKGR TRFYEQYGVI RDVLQNHLTE ALLFLVMELP ANASSAQELV QHKLQAFQSL
     WGLQRSSAVL GQYQAYDSQV QEELQEARGY VSTTPTFAGV LIHSQSPRWE GVPFLLTSGK
     ALDERVGYAR VLFKNKAYCP QSGTLRDAGH SQCKPKQIIF HFGHGALDAP AVLVSRNLFQ
     PVMPKDSWKE AGARSDLHIF GQPLSDFYMY SPVKERDAYS VVISNIYHGR KDFFITVEHL
     LASWAFWTPL LDSTSRQPPR LYPGGVENQQ LLDFEMVPGG VAFTLAEPAE LLNPGGQTPS
     DFRAIQSKFR QSPLVSGWAE ELIARLASDV EEAAVRSVAR SGRFHLALSG GSSPVGLFQR
     LARQHYGFPW QQSHVWLVDE RCVPLTDSES NFQGLHRHLL QHVRVPYFNI HPMPVHLNRR
     LCVEEDGGAQ LYAKDIVALV ANASFDLVLL GVGTDGHTAS LFPRSENGLE GAATVVLTES
     PVKPHQRMSL SLPLINRARQ VFVLVLGKGK HDITTLLSRV GHEPRKWPIS GVSPSSGQLV
     WYVDYEALLG
//
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