ID   A0A3Q3SHZ5_9TELE        Unreviewed;       823 AA.
AC   A0A3Q3SHZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) {ECO:0000313|Ensembl:ENSMAMP00000024945.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024945.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000024945.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC       {ECO:0000256|ARBA:ARBA00004959}.
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DR   AlphaFoldDB; A0A3Q3SHZ5; -.
DR   STRING; 205130.ENSMAMP00000024945; -.
DR   Ensembl; ENSMAMT00000025587.2; ENSMAMP00000024945.1; ENSMAMG00000016755.2.
DR   GeneTree; ENSGT00530000063435; -.
DR   InParanoid; A0A3Q3SHZ5; -.
DR   OrthoDB; 989808at2759; -.
DR   UniPathway; UPA00115; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..248
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          253..541
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   DOMAIN          592..814
FT                   /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01182"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   823 AA;  93398 MW;  D3E36F0CF66281F1 CRC64;
     MVVSLRQINF LQRTFRNCWE ETLLRVWMCW TSMLVIVFLL LVTLCAQGGN GEEREGAQRQ
     GHVSVMIVGG TGDLAKKYLW QGFFRLYINQ VGQGNTFSFY AGGLSPSDET TPIFFEILKA
     VSCSKDVSPE RCAILKDQFL RLSQYRQLKS LEDYQDLAKH IEKQLQEEGM TEAGRLFYLS
     VPAFAYADIA DKINSSCRPT SGAWLRVVLE KPFGHDFRSA QVLASQLRGS LQDEEMYRID
     HYLGKQVVAK ILPFRIENKK FLDPIWNKHH IERVEIVIKE ALNVKGRISF YDQYGVIRDM
     LQNHLTEIMT LLTMRPPKNL SSSEEVLQNK LHILSSVLPL GKNQAVIGQY QAYNSEVQQE
     LNKTKDHVSL TPTFAAVLAH IDEAQYEGVP VLLISGKMLD ERVGYARILF KNDIFCLENH
     NSIHCKPKQI VFYFGHGRLQ YPAILVSKNL FKPLSLNNEW KEVTEHTDIS VLGSPISDYY
     VQTPAEQREA YVELISHIYA GRKNSFISTE NLLASWDLWT PLLSSLASSF PRIYPGGVDN
     GNLLDIHLKG TAITYISEEV IISPDQMGGT SSNSFQVIHG KFRSADMVSA WAEELMERLA
     ADIQEAAEAA VHDGGVFHLA LSGGSSPLAL FHRLALHHFS FPWRNTHVWM VDERCVPQTE
     LESNFHTLHD HLLQHVRIPY YNIHPMPVQL NQRLCVEEDR GAQLYEKEIS KLVNGSSFHF
     VLLGVGYDGH TASLFPGSKI DALEENLVAL TESPVKPHQR MSLTFSAINR AHKVALLVMG
     KGKHEMVTQL SRVKDNLEKW PVTWVKPANG RLVWYIDYDA LLG
//