CAPPA_FLATR
ID CAPPA_FLATR Reviewed; 966 AA.
AC P30694; Q01648; Q42730;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=C4 phosphoenolpyruvate carboxylase {ECO:0000303|PubMed:10871630};
DE Short=C4 PEPC {ECO:0000303|PubMed:10871630};
DE Short=C4 PEPCase {ECO:0000303|PubMed:10871630};
DE Short=ppcA {ECO:0000303|PubMed:9225854};
DE EC=4.1.1.31 {ECO:0000269|PubMed:10871630, ECO:0000269|PubMed:12111227};
DE AltName: Full=Photosynthetic PEPCase {ECO:0000303|PubMed:10871630};
GN Name=PPCA {ECO:0000303|PubMed:9225854};
OS Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
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=4227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=1720398; DOI=10.1016/0014-5793(91)80850-3;
RA Poetsch W., Hermans J., Westhoff P.;
RT "Multiple cDNAs of phosphoenolpyruvate carboxylase in the C4 dicot Flaveria
RT trinervia.";
RL FEBS Lett. 292:133-136(1991).
RN [2]
RP SEQUENCE REVISION.
RA Poetsch W.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Bauwe H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP MUTAGENESIS OF LYS-600.
RX PubMed=7498490; DOI=10.1016/0014-5793(95)01189-l;
RA Gao Y., Woo K.C.;
RT "Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of
RT Flaveria trinervia: its roles in catalytic and regulatory functions.";
RL FEBS Lett. 375:95-98(1995).
RN [6]
RP MUTAGENESIS OF ARG-450; ARG-767 AND LYS-829.
RX PubMed=8774863; DOI=10.1016/0014-5793(96)00832-0;
RA Gao Y., Woo K.C.;
RT "Site-directed mutagenesis of Flaveria trinervia phosphoenolpyruvate
RT carboxylase: Arg450 and Arg767 are essential for catalytic activity and
RT Lys829 affects substrate binding.";
RL FEBS Lett. 392:285-288(1996).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9225854; DOI=10.1023/a:1005838020246;
RA Ernst K., Westhoff P.;
RT "The phosphoenolpyruvate carboxylase (ppc) gene family of Flaveria
RT trinervia (C4) and F. pringlei (C3): molecular characterization and
RT expression analysis of the ppcB and ppcC genes.";
RL Plant Mol. Biol. 34:427-443(1997).
RN [8]
RP CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-774, AND
RP PATHWAY.
RX PubMed=10871630; DOI=10.1074/jbc.m909832199;
RA Blasing O.E., Westhoff P., Svensson P.;
RT "Evolution of C4 phosphoenolpyruvate carboxylase in Flaveria, a conserved
RT serine residue in the carboxyl-terminal part of the enzyme is a major
RT determinant for C4-specific characteristics.";
RL J. Biol. Chem. 275:27917-27923(2000).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12111227; DOI=10.1007/s00425-002-0757-x;
RA Blasing O.E., Ernst K., Streubel M., Westhoff P., Svensson P.;
RT "The non-photosynthetic phosphoenolpyruvate carboxylases of the C4 dicot
RT Flaveria trinervia -- implications for the evolution of C4
RT photosynthesis.";
RL Planta 215:448-456(2002).
RN [10]
RP CHARACTERIZATION, MUTAGENESIS OF SER-774, AND DOMAIN.
RX PubMed=18266899; DOI=10.1111/j.1365-3040.2008.01796.x;
RA Jacobs B., Engelmann S., Westhoff P., Gowik U.;
RT "Evolution of C(4) phosphoenolpyruvate carboxylase in Flaveria:
RT determinants for high tolerance towards the inhibitor L-malate.";
RL Plant Cell Environ. 31:793-803(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH L-ASPARTATE, AND
RP ACTIVITY REGULATION.
RX PubMed=23443546; DOI=10.1038/ncomms2504;
RA Paulus J.K., Schlieper D., Groth G.;
RT "Greater efficiency of photosynthetic carbon fixation due to single amino-
RT acid substitution.";
RL Nat. Commun. 4:1518-1518(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH GLUCOSE-6-PHOSPHATE,
RP AND ACTIVITY REGULATION.
RX PubMed=24043710; DOI=10.1093/mp/sst130;
RA Schlieper D., Forster K., Paulus J.K., Groth G.;
RT "Resolving the activation site of positive regulators in plant
RT phosphoenolpyruvate carboxylase.";
RL Mol. Plant 7:437-440(2014).
CC -!- FUNCTION: Forms oxaloacetate through the carboxylation of
CC phosphoenolpyruvate (PEP). Catalyzes the first step of C4
CC photosynthesis. {ECO:0000269|PubMed:10871630,
CC ECO:0000269|PubMed:12111227}.
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:0000269|PubMed:10871630, ECO:0000269|PubMed:12111227};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9MAH0};
CC -!- ACTIVITY REGULATION: 5 fold activation by the allosteric regulator
CC glucose-6-phosphate (PubMed:24043710). Low sensitivity to inhibition by
CC L-malate and L-aspartate (PubMed:23443546). Up-regulated by light-
CC reversible phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:P04711, ECO:0000269|PubMed:23443546,
CC ECO:0000269|PubMed:24043710}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=27 umol/min/mg enzyme {ECO:0000269|PubMed:12111227};
CC -!- PATHWAY: Photosynthesis; C4 acid pathway. {ECO:0000269|PubMed:10871630,
CC ECO:0000269|PubMed:12111227}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9MAH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P27154}.
CC -!- TISSUE SPECIFICITY: Expressed in mesophyll cells, but not in bundle-
CC sheath, roots, stems and flowers. {ECO:0000269|PubMed:1720398,
CC ECO:0000269|PubMed:9225854}.
CC -!- DOMAIN: Region 2 (296-437) and region 5 (645-966) are involved in the
CC acquisition of C4-specific properties. Region 5 (645-966) is involved
CC in L-malate tolerance. {ECO:0000269|PubMed:18266899}.
CC -!- MISCELLANEOUS: Ser-774 is strongly involved in determining allosteric
CC behavior of C4 PEPC. {ECO:0000269|PubMed:10871630}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; X61304; CAA43601.1; -; mRNA.
DR EMBL; X64143; CAA45504.1; -; Genomic_DNA.
DR EMBL; Z25853; CAA81072.1; -; mRNA.
DR PIR; S18318; S18318.
DR PIR; S25082; S25082.
DR PIR; S37072; S37072.
DR PDB; 3ZGE; X-ray; 2.49 A; A/B=1-966.
DR PDB; 4BXC; X-ray; 2.86 A; A/B=1-966.
DR PDB; 4BXH; X-ray; 2.24 A; A/B=1-966.
DR PDBsum; 3ZGE; -.
DR PDBsum; 4BXC; -.
DR PDBsum; 4BXH; -.
DR AlphaFoldDB; P30694; -.
DR SMR; P30694; -.
DR PRIDE; P30694; -.
DR BRENDA; 4.1.1.31; 2270.
DR SABIO-RK; P30694; -.
DR UniPathway; UPA00322; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:UniProtKB.
DR GO; GO:0009760; P:C4 photosynthesis; TAS:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
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..966
FT /note="C4 phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166666"
FT ACT_SITE 172
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 600
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 641
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT BINDING 283
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 450
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 597
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 635
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 641
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:23443546,
FT ECO:0007744|PDB:3ZGE"
FT BINDING 665
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 673
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:23443546,
FT ECO:0007744|PDB:3ZGE"
FT BINDING 753
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 767..769
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:24043710,
FT ECO:0007744|PDB:4BXC"
FT BINDING 829
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:23443546,
FT ECO:0007744|PDB:3ZGE"
FT BINDING 888
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:23443546,
FT ECO:0007744|PDB:3ZGE"
FT BINDING 964
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:23443546,
FT ECO:0007744|PDB:3ZGE"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT MUTAGEN 450
FT /note="R->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:8774863"
FT MUTAGEN 600
FT /note="K->R,T: Decreased bicarbonate-binding and lower
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:7498490"
FT MUTAGEN 767
FT /note="R->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:8774863"
FT MUTAGEN 774
FT /note="S->A: Alteration of C4-specific kinetics, but no
FT effect on L-malate tolerance."
FT /evidence="ECO:0000269|PubMed:10871630,
FT ECO:0000269|PubMed:18266899"
FT MUTAGEN 829
FT /note="K->G: Decreased substrate binding and lower
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:8774863"
FT CONFLICT 77
FT /note="E -> D (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> P (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="L -> V (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> I (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="N -> KH (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="R -> Q (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="E -> K (in Ref. 4; CAA81072)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="C -> S (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="K -> N (in Ref. 3; CAA45504)"
FT /evidence="ECO:0000305"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:4BXH"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 202..220
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:4BXH"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:4BXH"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 296..324
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 364..389
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 453..466
FT /evidence="ECO:0007829|PDB:4BXH"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 477..488
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 503..517
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 534..546
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 562..577
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 579..585
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 588..593
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 604..624
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 628..633
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 644..651
FT /evidence="ECO:0007829|PDB:4BXH"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 668..675
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 678..697
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 705..726
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 732..739
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 742..746
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 762..765
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 782..785
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 788..798
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 801..812
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 814..828
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 832..842
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 848..869
FT /evidence="ECO:0007829|PDB:4BXH"
FT TURN 874..877
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 879..907
FT /evidence="ECO:0007829|PDB:4BXH"
FT HELIX 947..962
FT /evidence="ECO:0007829|PDB:4BXH"
SQ SEQUENCE 966 AA; 110406 MW; 252F7B674BC94F47 CRC64;
MANRNVEKLA SIDAQLRLLV PGKVSEDDKL VEYDALLLDK FLDILQDLHG EDLKEAVQQC
YELSAEYEGK HDPKKLEELG SLLTSLDTGD SIVIAKAFSH MLNLANLAEE LQIAYRRRIK
LKSGDFADEA NATTESDIEE TFKRLVHKLN KSPEEVFDAL KNQTVELVLT AHPTQSVRRS
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER FPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMT SNMYFSQIED LMIEMSMWRC NSELRVRAEE LYRTARKDVK HYIEFWKRIP
PNQPYRVILG DVRDKLYNTR ERSRHLLVDG KSDIPDEAVY TNVEQLLEPL ELCYRSLCDC
GDHVIADGSL LDFLRQVSTF GLSLVKLDIR QESDRHTEVL DAITQHLGIG SYREWSEEKR
QEWLLAELSG KRPLIGPDLP KTEEVKDCLD TFKVLAELPS DCFGAYIISM ATSTSDVLAV
ELLQREYHIK HPLRVVPLFE KLADLEAAPA AMTRLFSMDW YRNRIDGKQE VMIGYSDSGK
DAGRFSAAWQ LYKTQEQIVK IAKEFGVKLV IFHGRGGTVG RGGGPTHLAL LSQPPDTING
SLRVTVQGEV IEQSFGEEHL CFRTLQRFCA ATLEHGMNPP ISPRPEWREL MDQMAVVATE
EYRSVVFKEP RFVEYFRLAT PELEFGRMNI GSRPSKRKPS GGIESLRAIP WIFSWTQTRF
HLPVWLGFGA AFKHAIQKDS KNLQMLQEMY KTWPFFRVTI DLVEMVFAKG NPGIAALNDK
LLVSEDLRPF GESLRANYEE TKNYLLKIAG HKDLLEGDPY LKQGIRLRDP YITTLNVCQA
YTLKRIRDPN YHVTLRPHIS KEYAAEPSKP ADELIHLNPT SEYAPGLEDT LILTMKGIAA
GMQNTG
