CAPP1_FLAPR
ID CAPP1_FLAPR Reviewed; 967 AA.
AC Q01647;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=PPCA1;
OS Flaveria pringlei.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1508152; DOI=10.1007/bf00283848;
RA Hermans J., Westhoff P.;
RT "Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in
RT a C3 and a C4 Flaveria species.";
RL Mol. Gen. Genet. 234:275-284(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Svensson P., Blaesing O.E., Westhoff P.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC -!- PATHWAY: Photosynthesis; C3 acid pathway.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; X64144; CAA45505.1; -; Genomic_DNA.
DR EMBL; Z48966; CAA88829.1; -; mRNA.
DR PIR; S25081; S25081.
DR PIR; S52853; S52853.
DR PDB; 3ZGB; X-ray; 2.71 A; A/B=6-967.
DR PDBsum; 3ZGB; -.
DR AlphaFoldDB; Q01647; -.
DR SMR; Q01647; -.
DR PRIDE; Q01647; -.
DR BRENDA; 4.1.1.31; 2269.
DR SABIO-RK; Q01647; -.
DR UniPathway; UPA00321; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase;
KW Magnesium; Phosphoprotein; Photosynthesis.
FT CHAIN 1..967
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166664"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 601
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 291..292
FT /note="KH -> N (in Ref. 2; CAA88829)"
FT /evidence="ECO:0000305"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 202..220
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 247..264
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 297..325
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 365..390
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 444..453
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 454..467
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 478..489
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 504..518
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 535..547
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 563..577
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 580..586
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 596..603
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 605..626
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 645..652
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 679..698
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 706..727
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 733..740
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 743..748
FT /evidence="ECO:0007829|PDB:3ZGB"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 769..777
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 778..780
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 783..786
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 789..799
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 802..813
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 815..829
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 833..843
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 849..870
FT /evidence="ECO:0007829|PDB:3ZGB"
FT TURN 875..878
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 880..908
FT /evidence="ECO:0007829|PDB:3ZGB"
FT HELIX 948..963
FT /evidence="ECO:0007829|PDB:3ZGB"
SQ SEQUENCE 967 AA; 110629 MW; 8317EA8078C038C0 CRC64;
MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG EDLKEAVQEC
YELSAEYEGK HDPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
LKRGDFADEA NATTESDIEE TFKKLVLKLN KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG KHPRVTPEVT
RDVCLLARMM ASNMYFSQIE DLMFEMSMWR CNSELRVRAE ELYRTARRDV KHYIEFWKQV
PPTEPYRVIL GDVRDKLYNT RERSRHLLAH GISDIPEEAV YTNVEQFLEP LELCYRSLCD
CGDRVIADGS LLDFLRQVST FGLSLVKLDI RQESDRHTDV LDAITQHLEI GSYREWSEEK
RQEWLLAELS GKRPLFGSDL PKTEEVKDVL DTFNVLAELP SDCFGAYIIS MATSPSDVLA
VELLQRECHV KHPLRVVPLF EKLADLEAAP AAMARLFSID WYRNRIDGKQ EVMIGYSDSG
KDAGRFSAAW QLYKAQEEII KVAKEFGVKL VIFHGRGGTV GRGGGPTHLA ILSQPPDTIH
GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP PISPRPEWRE LMDQMAVVAT
EEYRSIVFKE PRFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR
FHLPVWLGFG AAFKHAIKKD SKNLQMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND
KLLVSEDLWP FGESLRANYE ETKDYLLKIA GHRDLLEGDP YLKQRIRLRD SYITTLNVCQ
AYTLKRIRDP NYHVTLRPHI SKEYAAEPSK PADELIHLNP TSEYAPGLED TLILTMKGIA
AGMQNTG
