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Database: UniProt
Entry: A0A087QL65_APTFO
LinkDB: A0A087QL65_APTFO
Original site: A0A087QL65_APTFO 
ID   A0A087QL65_APTFO        Unreviewed;       772 AA.
AC   A0A087QL65;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=GDH/6PGL endoplasmic bifunctional protein {ECO:0000313|EMBL:KFM01969.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_13015 {ECO:0000313|EMBL:KFM01969.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM01969.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM01969.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM01969.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC       {ECO:0000256|ARBA:ARBA00004959}.
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DR   EMBL; KL225737; KFM01969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087QL65; -.
DR   STRING; 9233.A0A087QL65; -.
DR   UniPathway; UPA00115; -.
DR   Proteomes; UP000053286; 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:UP000053286}.
FT   DOMAIN          11..193
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          199..489
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   DOMAIN          541..763
FT                   /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01182"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM01969.1"
FT   NON_TER         772
FT                   /evidence="ECO:0000313|EMBL:KFM01969.1"
SQ   SEQUENCE   772 AA;  87220 MW;  EE2D4E2D607D1CFB CRC64;
     AEVSQGHISV VLLGATGDLA KKYLWQGLFQ LYMDQVSSGH SFTFHGAALT ALEPGQRLMF
     DVLKKLACPP DESPNRCAVL KDQFLKLSQY HQLKTAENYT VLNREIETLL RQEGLKEAGR
     IFYFSVPPFA YTEIARHINS SCRPPPGAWL RVVLEKPFGH DLESAQQLAA ELTSFFREEE
     MYRVDHYLGK QAVAHILPFR DHNRQFLDPI WNRHHVERVE IVLKETVDAK GRTSFYEQYG
     VIRDVLQNHL TEALMFLTME LPANVSSAEE VLQRKLQAFQ FLRGLEKNSV VLGQYQAYAS
     QVQEELQKAQ DYISTTPTFA GVLIHSDSLR WEGVPFLLTS GKALDERVGY VRVLFKNQAY
     CTQSETLRDA GHSQCKAKQI IFYIGHGALK TPAVLVSRNL FRPVMPEGSW REAVGQSDLH
     IFGQPLSDYY VYSPVKERDA YSVLISNIYH GRKDFFITTE NLLASWGFWT PLLDSISHQP
     LRLYPGGVEN QDLLDFEMVS GEVAFTLAEP VELLNPNGLM PSEYRTIQSK FRQSPLVSAW
     SEDLISQLAS DIEKTASRTV AHSGQFHLAL SGGSSPVVLF QQLARHHYAF PWKHTHIWLV
     DERCVPLSDT ESNFFSLHNH LLQNVRVPYF NVHPMPVHLN QRLCVEEDRG TELYAKEIMA
     LVANASFDLV LLGVGTDGHT ASLFPQSENG LEGAQTVVLT ESPVKPHQRM SLSLPVINKA
     RQVFVLVLGK GKHNITTLLS RVGHEPRKWP ISGVSPSSGQ LVWYVDYEAL LG
//
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