ID A0A445CN56_ARAHY Unreviewed; 1089 AA.
AC A0A445CN56;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN ORFNames=Ahy_A06g027291 {ECO:0000313|EMBL:RYR52362.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR52362.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR52362.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR52362.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. {ECO:0000256|RuleBase:RU362120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000256|RuleBase:RU362120};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005527}.
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:RYR52362.1}.
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DR EMBL; SDMP01000006; RYR52362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445CN56; -.
DR STRING; 3818.A0A445CN56; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000289738; Chromosome a06.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14137; STKc_GSK3; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR PANTHER; PTHR24057:SF69; SHAGGY-RELATED PROTEIN KINASE GAMMA; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Carbohydrate metabolism {ECO:0000256|RuleBase:RU362120};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW NADP {ECO:0000256|RuleBase:RU362120};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Oxidoreductase {ECO:0000256|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 70..354
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1089 AA; 122538 MW; DE000DD1AFABBF70 CRC64;
MASVGMAPTS GVRESGGGVD RLPEEMNDMK IRDDKEMEAT VVDGNGTETG HIIVTTIGGR
NGQPKQTISY MAERVVGHGS FGVVFQAKCL ETGETVAIKK VLQDKRYKNR ELQTMRLLDH
PNVVSLKHCF FSTTEKDELY LNLVLEYVPE TVSRVIKHYN KLSQRMPLIY VKLYTYQIFR
ALSYIHRCIG VCHRDIKPQN LLVNPHTHQV KLCDFGSAKV LVKGEPNISY ICSRYYRAPE
LIFGATEYTT AIDVWSVGCV LAELLLGQPL FPGESGVDQL VEIIKVLGTP TREEIKCMNP
NYTEFKFPQI KAHPWHKIFH KRMPPEAVDL VSRLLQYSPN LRCSALDALT HPFFDELRDP
NARLPNGRFL PPLFNFKAHG GSSGGIGEID SRVCEEAMPV SRLIEIYIGT QIFYPMLDGY
SEEHRPCFHV QQQIVTSNRR PKCHVLYICG YNDGVADLVM LSMLVSSDYN SVVSIILGQK
QTFKSSTTVK SFKSHLSNIK EVAGMSLSFS SASVALSECS IPIHRCCHAH RVTGGSRSLS
SVTGSDRLVL NVRNGNLCRK FRGLKLWILE RLNFQIQPAK LHKRSTNGSQ DRIHHFKNNL
ETGSSPSITH THVIPHDKVS SISMDVSGGP SLCIAVIGAT GELARGKIFP ALFALYYSGF
LPQNVGIFGY SRKDMTDEDL RFCIASTLTC RVDHQENCGD KMDAFLNRTY YINGGYDNKH
GMSMLNARME QIEGGSKANR IFYLSVPQEA LLDVASCLAS NAQTQSGWNR IIIEKPFGFD
VLSSHRLTQS LLSKYEEKQI YRIDHLLGRN LIENLTVLRF ANLVFEPLWS RTYIHNIQII
LSEELGVQPG RYFSGYGIIR DIVHSHVLQT IALLAMEPPI SLDGEDIRNE KVKVLRSIRK
LEPRDVILGQ YKASSKDKVD VCVNGLTPTY FAAAMYIDNA RWDGVPFLVK TGFGLIKHQM
EIRIQFRHVP GNVYDESIGH NIDRAANELI LRDVPDEAIL VKVNNKIPGL GYNMEVPDSY
EHLLLDVIDG DNHLFMRSDE LAAAWNIISP ILNEMDKDNM SLELYELGGR GPVGAYYLWA
KHGVRWVED
//
