G6PD4_ARATH
ID G6PD4_ARATH Reviewed; 625 AA.
AC Q93ZW0; O80525;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Inactive glucose-6-phosphate 1-dehydrogenase 4, chloroplastic {ECO:0000305};
DE Short=AtG6PD4 {ECO:0000303|PubMed:15634201};
DE Short=G6PDH4 {ECO:0000305};
DE Flags: Precursor;
GN Name=G6PD4 {ECO:0000303|PubMed:15634201};
GN OrderedLocusNames=At1g09420 {ECO:0000312|Araport:AT1G09420};
GN ORFNames=F14J9.8 {ECO:0000312|EMBL:AAC33202.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15634201; DOI=10.1111/j.1365-313x.2004.02293.x;
RA Wakao S., Benning C.;
RT "Genome-wide analysis of glucose-6-phosphate dehydrogenases in
RT Arabidopsis.";
RL Plant J. 41:243-256(2005).
RN [5]
RP FUNCTION, INTERACTION WITH G6PD1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-212 AND CYS-220.
RX PubMed=21309870; DOI=10.1111/j.1365-313x.2011.04535.x;
RA Meyer T., Hoelscher C., Schwoeppe C., von Schaewen A.;
RT "Alternative targeting of Arabidopsis plastidic glucose-6-phosphate
RT dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in
RT the cytosol.";
RL Plant J. 66:745-758(2011).
CC -!- FUNCTION: Seems to be a catalytically inactive enzyme.
CC {ECO:0000269|PubMed:21309870}.
CC -!- SUBUNIT: Forms homodimer (By similarity). Interacts with G6PD1
CC (PubMed:21309870). {ECO:0000250|UniProtKB:P11411,
CC ECO:0000269|PubMed:21309870}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21309870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q93ZW0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and buds.
CC {ECO:0000269|PubMed:15634201}.
CC -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in
CC A.thaliana. {ECO:0000303|PubMed:15634201}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003970; AAC33202.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28440.1; -; Genomic_DNA.
DR EMBL; AY056232; AAL07081.1; -; mRNA.
DR EMBL; AY117271; AAM51346.1; -; mRNA.
DR PIR; E86227; E86227.
DR RefSeq; NP_563844.1; NM_100813.2. [Q93ZW0-1]
DR AlphaFoldDB; Q93ZW0; -.
DR SMR; Q93ZW0; -.
DR BioGRID; 22706; 2.
DR STRING; 3702.AT1G09420.2; -.
DR PaxDb; Q93ZW0; -.
DR PRIDE; Q93ZW0; -.
DR ProteomicsDB; 230469; -. [Q93ZW0-1]
DR EnsemblPlants; AT1G09420.1; AT1G09420.1; AT1G09420. [Q93ZW0-1]
DR GeneID; 837465; -.
DR Gramene; AT1G09420.1; AT1G09420.1; AT1G09420. [Q93ZW0-1]
DR KEGG; ath:AT1G09420; -.
DR Araport; AT1G09420; -.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_1_0_1; -.
DR InParanoid; Q93ZW0; -.
DR PhylomeDB; Q93ZW0; -.
DR BioCyc; ARA:AT1G09420-MON; -.
DR BRENDA; 1.1.1.49; 399.
DR PRO; PR:Q93ZW0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93ZW0; baseline and differential.
DR Genevisible; Q93ZW0; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW Glucose metabolism; NADP; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..625
FT /note="Inactive glucose-6-phosphate 1-dehydrogenase 4,
FT chloroplastic"
FT /id="PRO_0000010438"
FT BINDING 160..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT DISULFID 212..220
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
FT MUTAGEN 212
FT /note="C->S: Abolishes interaction with G6PD1."
FT /evidence="ECO:0000269|PubMed:21309870"
FT MUTAGEN 220
FT /note="C->S: Abolishes interaction with G6PD1."
FT /evidence="ECO:0000269|PubMed:21309870"
SQ SEQUENCE 625 AA; 70202 MW; 83D9F8D96F0B66F4 CRC64;
MSLSSCLLPF SQSATAPSSS VCSCHLAASF SNFPVSSRDY SFSRSGSLVL NGGGSNLCRR
FCGLKLWILK SLNRRQGNNR KHQPVNELTT HSKHTFLSDD ERGFAEETRA EDLRPEENIL
GTDLNDGFHN VGDLPPVSKQ LSDDLSDVRR RASLCIAVVG ATGELARGKI FPALFALYYS
GYLPEDVAIF GVSRKNLTDE DLRSIIASTL TCRVDHQENC GGKMDAFQSR TYYINGGYNN
RDGMSRLAER MKQIEGESEA NRIFYLSVPQ EALVDVACTI GDNAQAPRGW TRIIVEKPFG
FNSHSSHQLT KSLLSKFEEK QIYRIDHMLG RNLIENLTVL RFSNLVFEPL WNRTYIRNIQ
VIISESIAQT EKFSDGYGII RDIVHSHILQ TIALLAMEPP ISLDGEDIRN EKVKVLRSIR
KIDPRDVILG QYKSSSRDKN GVILNGVDPT YCAAALYIDN ARWDGVPFLV RVGTGLIKHR
VEIHVQFRHV PGNLYRENIG INIDLGTNEL ILRDEPDEAI LVKINNKVPG LGLQLDASEL
NLLYKDRYKT EVPDSYEHLI HDVIDGDNHL FMRSDEVAAA WNILSPVLEE IDKHHTAPEL
YEFGGRGPVA AYYLWAKHGV PWADD
