ID A0A087GCM5_ARAAL Unreviewed; 451 AA.
AC A0A087GCM5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Pyruvate carboxyltransferase domain-containing protein {ECO:0000259|PROSITE:PS50991};
GN OrderedLocusNames=AALP_Aa8g407800 {ECO:0000313|EMBL:KFK27627.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK27627.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CM002876; KFK27627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GCM5; -.
DR EnsemblPlants; KFK27627; KFK27627; AALP_AA8G407800.
DR Gramene; KFK27627; KFK27627; AALP_AA8G407800.
DR eggNOG; KOG2367; Eukaryota.
DR OrthoDB; 375at2759; -.
DR Proteomes; UP000029120; Chromosome 8.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR10277:SF60; METHYLTHIOALKYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 2.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 81..312
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 451 AA; 49632 MW; A8F7328F0D516537 CRC64;
MASSLLTSSG MISTTGSTVV VQSLLPFRSL RLIRPYNKQS LFISCCSSVS KKVAISAIDV
NPVVERWPEY IPNKLPDKNY VRVLDTTLRD GEQAPGGALT PSQKLEIARQ LAKLRVDIME
VGFPASSEEE FEAVKTIAKT VGNEVDEDTG YVPSICVIAR CKQRDIEIAW ESVKWWQVGE
GVYMHGFRRS DKSGCNHGDN RGHSRDQHAA RTRRTWINMP QELGELVSYV LANTPGIDDV
VFGIHCHNDL GLATANSLAG ICAGARQVEV TVNGIGERSG NAPLEEVVMA LKCRGAYLMD
GAYTRIDSRQ IMATSKMVQE YTGLYVQPHK PIVGDNCFVH ESGIHQDGIL KNRSTYEILS
PEDVGIVISQ NSGILLGKLS GRHAVKGRLK ELGYEIDDKK LNDIFSRFRD LTKQKKRITD
ADLKSLVTCS DKIPSEISNG SIPIPQISSV V
//
