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Database: UniProt
Entry: H3DBA1_TETNG
LinkDB: H3DBA1_TETNG
Original site: H3DBA1_TETNG 
ID   H3DBA1_TETNG            Unreviewed;       489 AA.
AC   H3DBA1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) {ECO:0000313|Ensembl:ENSTNIP00000017793.1};
GN   Name=H6PD {ECO:0000313|Ensembl:ENSTNIP00000017793.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000017793.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000017793.1}
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; H3DBA1; -.
DR   STRING; 99883.ENSTNIP00000017793; -.
DR   Ensembl; ENSTNIT00000018017.1; ENSTNIP00000017793.1; ENSTNIG00000014756.1.
DR   GeneTree; ENSGT00530000063435; -.
DR   HOGENOM; CLU_013524_2_0_1; -.
DR   InParanoid; H3DBA1; -.
DR   OMA; YCPQSGT; -.
DR   TreeFam; TF354247; -.
DR   UniPathway; UPA00115; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
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   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   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:UP000007303}.
FT   DOMAIN          15..197
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          202..474
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   489 AA;  55194 MW;  53ECDF51DEED672A CRC64;
     EDRKDGQAPG HVSVVVVGGT GDLAKKYLWQ GFFSLYADKV SSGNTFSFVC GGLSPPDRAT
     PVFFEILKGL SCWKAVSEER CALLKEQFLR LSQYRQLKTL EQYQDLNKHI EQELQQEGMR
     EAGRLFYLSV PAFAYADVAD KINSSCRPKS GAWLRVVLEK PFGHDLRSAQ VLTSQLESSL
     KDEEMYRIDH YLGKQAVAKI LPFRMDNSGF LDPIWNKNHI ERVEVVVKET LDVKGRISYY
     DQYGVIRDML QNHMTEVMTL LTMRLPSSRD SSDEVLRNQL QVLGSLQPLG RRQAVVGQYQ
     SYRSEVQQEL NKTREHVSLT PTFAAVLAFS GEARYDGVPI LLVSGKKLDE RVGYARILFK
     NDVLCLQNHP GVHCKPKQIV FHFGHGALGH PAILVSKNLF KPLLKDAEQR EAYSELISHI
     FAGRKNNFIR AESLLASWGL WTPLLSGLAD TFPRIYPGGA ENGASLDVYV KGNELRFYTE
     VTIINSDPM
//
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