ID A0A1Z5RA41_SORBI Unreviewed; 884 AA.
AC A0A1Z5RA41;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=SORBI_3007G106500 {ECO:0000313|EMBL:OQU80295.1};
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:OQU80295.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU80295.1, 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; CM000766; OQU80295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5RA41; -.
DR EnsemblPlants; OQU80295; OQU80295; SORBI_3007G106500.
DR Gramene; OQU80295; OQU80295; SORBI_3007G106500.
DR Proteomes; UP000000768; Chromosome 7.
DR ExpressionAtlas; A0A1Z5RA41; baseline and differential.
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 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:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 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 91
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 884 AA; 100853 MW; 236146EAF294AD0A CRC64;
MLTSLDPGDS IVTAKAFSHM LNLANLAEEV QIAYRRRIKL KKGDFADENS ALTESDIEET
FKRLVVDLKK SPAEVFDALK SQTVDLVLTA HPTQSVRRSL LQKHSRIRNC LVQLCSKDIT
PDDKQELDEA LQREIQAAFR TDEIRRTQPT PQDEMRAGMS YFHETIWKGV PKFLRRVDTA
LKNIGIDERV PYNAPLIQFS SWMGGDRDGN PRVTPEVTRD VCLLARMMAA NLYCSQIENL
MFELSMWRCN DELRAQADEL HRSSKKDAKH YIEFWKKVPP SEPYRVILGD LRDKLYNTRE
RARQLLSSGY SDIPEESTVT NVEQFLEPLE LCYRSLCACG DRVIADGSLL DFLRQVSTFG
LCLVRLDIRQ ESDRHTDVLD AITTYLGIGS YREWSEERRQ EWLLSELNGK RPLFGPDLPT
TDEIADVLDT FRVIAELPAD NFGAYIISMA TAPSDVLAVE LLQRECHVKT PLRVVPLFEK
LADLEGAPAA LARLFSVDWY RERINGKQEV MIGYSDSGKD AGRLSAAWQL YKAQEELIKV
AKKFGVKLTM FHGRGGTVGR GGGPTHLAIL SQPPDTIHGS LRVTVQGEVI EQSFGEEHLC
FRTLQRFTAA TLEHGMHPPI SPKPEWRALL DEMAVVATKE YRSIVFQEPR FVEYFRLATP
EMEYGRMNIG SRPSKRKPSG GIESLRAIPW IFAWTQTRFH LPVWLGFGAA FKHILEKDIR
NLHMLQEMYN EWPFFRVTID LVEMVFAKGD PGIAALYDKL LVSSELWPLG EKLRANYEET
KRLLLQVAGH KDLLEGDLYL KQRLRLRDAY ITTLNVCQAY TMKRIRDPDY HVTLRPHLSK
EIMDWNKPAA ELVKLNPTSE YAPGLEDTLI LTMKGIAAGM QNTG
//
