CAPP_SYNY3
ID CAPP_SYNY3 Reviewed; 1034 AA.
AC P74299;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppc; OrderedLocusNames=sll0920;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000022; BAA18393.1; -; Genomic_DNA.
DR PIR; S76134; S76134.
DR AlphaFoldDB; P74299; -.
DR SMR; P74299; -.
DR DIP; DIP-48802N; -.
DR IntAct; P74299; 5.
DR STRING; 1148.1653480; -.
DR PaxDb; P74299; -.
DR PRIDE; P74299; -.
DR EnsemblBacteria; BAA18393; BAA18393; BAA18393.
DR KEGG; syn:sll0920; -.
DR eggNOG; COG2352; Bacteria.
DR InParanoid; P74299; -.
DR OMA; PWVFGWT; -.
DR PhylomeDB; P74299; -.
DR BRENDA; 4.1.1.31; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT CHAIN 1..1034
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166642"
FT ACT_SITE 203
FT /evidence="ECO:0000250"
FT ACT_SITE 680
FT /evidence="ECO:0000250"
SQ SEQUENCE 1034 AA; 118940 MW; 76DF6061BAB7235D CRC64;
MNLAVPAFGL STNWSGNGNG SNSEEESVLY QRLKMVEELW ERVLQSECGQ ELVDLLTELR
LQGTHEAITS EISEEVIMGI TQRIEHLELN DAIRAARAFA LYFQLINIVE QHYEQNEQQR
NRWEASQETN FYEQAGNEEE MVPPSRLGAS TEPLPVGIDQ NELQASVGTF HWLMRELKRL
NVPPQHIQNL LDHLDIRLVI TAHPTEIVRH TIRRKQRRVD RILRKLDQLQ GSVTGRDWLN
TWDAKTAIAQ LTEEIRFWWR TDELHQFKPT VLDEVDYSLH YFDEVLFDAV PELSKRLGQA
IKETFPHLRA PRANFCYFGS WVGGDRDGNP SVTPEVTWQT ACYQRGLVLG KYLFSLGELV
AILSPSLHWC KVSQELLDSL ERDRIQLPEI YEELSLRYRQ EPYRMKLAYV TKRLENTLRR
NNRLANPEER QTMITMPAEN HYRTGEELLE ELRLIQRNLT ETGLTCLELE NLITQLEVYG
FNLAQLDFRQ ESSRHAEAIA EIAEYMGVLT TPYEEMAEED KLAWLGVELQ TRRPLIPQEM
PFSERTRETI ETLRTLRHLQ MEFGVDICQT YIISMTNDAS DVLEVLLLAK EAGLYDPATA
SNSLRIVPLF ETVEDLKNAP GIMDSLFSLP FYRATLAGSY HSLKELQNQP PDYYQIPTTT
ALLNPGNLQE IMVGYSDSNK DSGFLSSNWE IHKAQKSLQA VAQSHRVILR LFHGRGGSVG
RGGGPAYKAI LAQPAGTVDG RIKITEQGEV LASKYSLPEL ALYNLETLTT AVIQASLLKS
SFDFIEPWNR IMEELACTAR RAYRSLIYEE PDFLDFFLTV TPIPEISELQ ISSRPARRKG
GKADLSSLRA IPWVFSWTQT RFLLPAWYGV GTALKSFVDQ DPVKNMKLLR YFYFKWPFFN
MVISKVEMTL SKVDLTIASH YVQELSKPED RERFDRLFQQ IKQEYQLTRD FAMEITAHPH
LLDGDRSLQR SVLLRNRTIV PLGLLQISLL KRLRQVTQEA ETSGVRYRRY SKEELLRGAL
LTINGIAAGM RNTG