ID U5HTH1_MANES Unreviewed; 965 AA.
AC U5HTH1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN Name=PEPC {ECO:0000313|EMBL:AFN70424.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:AFN70424.1};
RN [1] {ECO:0000313|EMBL:AFN70424.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AFN70424.1};
RA Zhang Y., Chen X., Lu C., Wang W.-Q.;
RT "Cloning and Expression Analysis of Phosphoenolpyruvate Carboxylase Gene
RT pepc from Cassava (Manihot esculenta Crantz).";
RL J Trop Subtrop Botany 20:369-375(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR EMBL; JN387052; AFN70424.1; -; mRNA.
DR AlphaFoldDB; U5HTH1; -.
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: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:SF47; PHOSPHOENOLPYRUVATE CARBOXYLASE 2; 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 2: Evidence at transcript level;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyruvate {ECO:0000313|EMBL:AFN70424.1}.
FT ACT_SITE 172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 965 AA; 110360 MW; E7600C1E126E3FEB CRC64;
MAARNLEKMA SIDAQLRLLA PRKVSEDDKL VEYDALLLDR FLDISQDLHG EEIRETVQDC
YELSAEYEGK HDPQKLEELG KVLTSLDPGD SIVVAKSFSH MLNLANLAEE VQIAYGRRIK
LKKGDFADEN SATTESDIEE TLKRLVVQLK KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKHARIRN CLTQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER IPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANLYFSQIED LMFELSMWRC NDELRVHADE LHRSSRRDAK HYIEFWKQIP
ASEPYRVILG DVRDKLYNTR ERSRHLLVNG ISDIPEEATF TNVEQFLQPL ELCYRSLCAC
GDRPIADGSL LDFLRQVSTF GLSLVRLDIR QESDRHTDVL DAITKYLGIG SYREWSEESR
QEWLLSELRG KRPLFGPDLP KTEEIADVLD TFHVIAELPP DNFGAYIISM ATAPSDVLAV
ELLQRECHVK QPLRVVPLFE KLADLEAAPA AVARLFSVDW YRNRINGKQE VMIGYSDSGK
DAGRLSAAWQ LYKAQEELVK VAKQYGVKLT MFHGRGGTVG RGGGPTHLAI LSQPPDTIHG
SLRVTVQGEV IEQSFGEEHL CFRTLQRFTA ATLEHGMHPP ISPKPEWRAL MDEMAIIATK
EYRSIVFQEP RFVEYFRLAT PELEYGRMNI GSRPSKRKPS GGIESLRAIP WIFAWTQTRF
HLPVWLGFGA AFRHVVEKDI KNLQMLQEMY NQWPFFRVTI DLVEMVFAKG DPGIAALYDK
LLVSKELWPF GERLRANYEE TKSFLLKIAG HKDLLEGDPY LKQRLRLRDA YITTLNVCQV
YTLKRIRDPD YYVTVRPHLS KEYMESTKPA AELVKLNPTS EYAPGLEDTL ILTMKGIAAG
MQNTG
//