ID C5XYZ9_SORBI Unreviewed; 960 AA.
AC C5XYZ9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=SORBI_3004G106900 {ECO:0000313|EMBL:EES04831.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES04831.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES04831.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003774}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR EMBL; CM000763; EES04831.1; -; Genomic_DNA.
DR RefSeq; XP_002451855.1; XM_002451810.1.
DR AlphaFoldDB; C5XYZ9; -.
DR SMR; C5XYZ9; -.
DR STRING; 4558.C5XYZ9; -.
DR EnsemblPlants; EES04831; EES04831; SORBI_3004G106900.
DR GeneID; 8078313; -.
DR Gramene; EES04831; EES04831; SORBI_3004G106900.
DR KEGG; sbi:8078313; -.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; C5XYZ9; -.
DR OMA; PSFEVMP; -.
DR OrthoDB; 355614at2759; -.
DR BRENDA; 4.1.1.31; 5768.
DR Proteomes; UP000000768; Chromosome 4.
DR ExpressionAtlas; C5XYZ9; baseline and differential.
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:0048366; P:leaf development; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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:SF48; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 1.
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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT ACT_SITE 168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 596
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 960 AA; 109366 MW; 08F9C283CE3734C4 CRC64;
MPERHQSIDA QLRLLAPGKV SEDDKLVEYD ALLVDRFLDI LQDLHGPHLR EFVQECYELS
AEYENDRDEA RLGELGSKLT SLPPGDSIVV ASSFSHMLNL ANLAEEVQVA QRRRIKLKRG
DFADEASAPT ESDIEETLKR LVSQLGKSRE EVFDALKNQT VDLVFTAHPT QSVRRSLLQK
HGRIRNCLRQ LYAKDITADD KQELDEALQR EIQAAFRTDE IRRTPPTPQD EMRAGMSYFH
ETIWKGVPKF LRRIDTALKN IGINERLPYN APLIQFSSWM GGDRDGNPRV TPEVTRDVCL
LARMMAANLY FSQIEDLMFE LSMWRCSDEL RIRADELHRS SKRAAKHYIE FWKQVPPNEP
YRVILGDVRD KLYYTRERSR HLLSSGISEI PEEATFTNVE QFLEPLELCY RSLCACGDKP
IADGSLLDFL RQVSTFGLAL VKLDIRQESD RHTDVLDSIT THLGIGSYAE WSEEKRQDWL
LSELRGKRPL FGSDLPQTEE TADVLGTFHV LAELPADCFG AYIISMATAP SDVLAVELLQ
RECHVKQPLR VVPLFEKLAD LEAAPAAVAR LFSIDWYMNR INGKQEVMIG YSDSGKDAGR
LSAAWQMYKA QEELIKVAKH YGVKLTMFHG RGGTVGRGGG PTHLAILSQP PDTIHGSLRV
TVQGEVIEHS FGEELLCFRT LQRYTAATLE HGMHPPISPK PEWRALMDEM AVVATKEYRS
IVFQEPRFVE YFRSATPETE YGRMNIGSRP SKRKPSGGIE SLRAIPWIFA WTQTRFHLPV
WLGFGAAIKH IMQKDIRNIH VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI AAVYDKLLVA
EDLQSFGEQL RKNYEETKEL LLQVAGHKDV LEGDPYLKQR LRLRESYITT LNVCQAYTLK
RIRDPSFQVS PQPPLSKEFT DESQPVELVQ LNQQSEYAPG LEDTLILTMK GIAAGMQNTG
//
