ID A0A059D6N8_EUCGR Unreviewed; 1059 AA.
AC A0A059D6N8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=EUGRSUZ_B03067 {ECO:0000313|EMBL:KCW86388.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW86388.1, ECO:0000313|Proteomes:UP000030711};
RN [1] {ECO:0000313|Proteomes:UP000030711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR EMBL; KK198754; KCW86388.1; -; Genomic_DNA.
DR RefSeq; XP_010044308.1; XM_010046006.2.
DR AlphaFoldDB; A0A059D6N8; -.
DR STRING; 71139.A0A059D6N8; -.
DR EnsemblPlants; KCW86388; KCW86388; EUGRSUZ_B03067.
DR GeneID; 104433317; -.
DR Gramene; KCW86388; KCW86388; EUGRSUZ_B03067.
DR KEGG; egr:104433317; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR InParanoid; A0A059D6N8; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000030711; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 2.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000030711}.
FT REGION 326..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 726
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1059 AA; 119529 MW; A3BC2D25C1BA19FE CRC64;
MTDTTDDIAE EISFQNFDDD CKLLGNLLND VLQREVGAKF MEKIERNRIL AQSACNMRTA
GIEDAAELLE KQLASEISKM TLEEALTLAR AFSHYLNLMG IAETHHRVRK SRNFTLLSRS
CDDIFSQMIQ GGVSPDELYD TVCKQEVEIV LTAHPTQINR RTLQYKHIRI AHLLDYNDRP
DLTHEDREML IEDLVREITA IWQTDELRRH KPTPVDEARA GLNIVEQSLW KAIPHYLRRV
SSALKKHTGR PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT KDVSLLSRWM AIDLYIREVD
SLRFELSMNR CSDRLLRLAH EILEKETSSE DRLESRSQSL TRSQIKLNNQ QLPSLPTQLP
AGADMPSCTE CNDGDSQYPR LELPGTDYMP LNRQEGQGPS FSDSQFQDSG RSSSKSSENG
TSSNGLQPAV TPRGSSYASS QFHAQRKLFA ESQIGRSSFH KLLEPSLPQL PGIAPYRIVL
GDVKDKLMKT RRRLELRLED LPCEHDFCDY YESSDQLLEP LILCYESLQS CGSGVLADGR
LADLIRRVAT FGIVLMKLDL RQESGRHSET LDAITRYLDM GTYSEWDEEK RLEFLTRELK
GKRPLVPPSI EVAPDIREVL DTFRVAAELG SDSLGAYVIS MASNASDVLA VELLQKDARL
AVSGELGRPC LGGTLRVVPL FETVKDLREA GSVIRKLLSI DWYREHILRN HGGHQEVMVG
YSDSGKDAGR FTAAWELYKA QEDVVAACNE YDIKVTLFHG RGGSIGRGGG PTYLAIQSQP
PGSVMGTLRS TEQGEMVQAK FGLPQTAVRQ LEIYTTAVLL ATLRPPLSPR EEKWRNLMEE
ISKISCQSYR NTVYENPEFL AYFHEATPQA ELGFLNIGSR PTRRKSSTGV GHLRAIPWVF
AWTQTRFVLP AWLGVGAGLR GVCEKGHTAE LQEMYKEWPF FQSTVDLIEM VLGKADIPIA
KHYDEVLVSE SRRELGAELR RELLTTEKYV LVISGHEKLS ENNRSLRRLI ESRLPYLNPM
NMLQVEILKR LRRDDDNNKL RDALQITFNG IAAGMRNTG
//