ID   CAPP_PARMW              Reviewed;        1010 AA.
AC   Q7U4M0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=SYNW2047;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; BX569694; CAE08562.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U4M0; -.
DR   SMR; Q7U4M0; -.
DR   STRING; 84588.SYNW2047; -.
DR   KEGG; syw:SYNW2047; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000001422; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
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   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:SF6; 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   Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..1010
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166639"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        652
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   1010 AA;  114491 MW;  5518FAF67411F83A CRC64;
     MIMRSPETSG ASMPQSTAHV PDGEQPRASG GSPGAGRLLQ HRLELVEDLW QTVLRSECPP
     EQSERLLRLK QLSDPVALEG RDGESSSEAI VELIRSMDLS EAIAAARAFS LYFQLINILE
     QRIEEDSYLD SLRPSRSQDD ETAAPFDPFA PPLASQTDPA TFGEVFERLR RMNVPPAQVE
     TLLRELDIRL VFTAHPTEIV RHTVRHKQRK VASLLQRLQS EPALPRYDEE ELRRQLEEEI
     RLWWRTDELH QFKPTVLDEV DSTLHYFQQV LFEAMPQLRR RLVSSLSRHY PDVQFPQASF
     CTFGSWVGSD RDGNPSVTPE ITWRTACYQR QLMLELYIGS VQSLRNQLSI SMQWSQVAPP
     LLESLEMDRL RFPEIYERRA ARYRLEPYRL KLSYILERLE LTLQRNHQMS EAGWQSPPEP
     AATAPTDGIP GHEALHYTAI DQFRSDLELI RNSLVSTELS CEQLDTLLNQ VHIFGFSLAS
     LDIRQESTRH SDAIDELTTH LQLPKAYGAM EESERVAWLL EELQTRRPLI PAAVEWSEAT
     AQTFAVFQML HRLQQEFGQR ICHSYVISMS HTASDLLEVM LLAKEIGLVD PQAGKASLLV
     VPLFETVEDL QRAPAVMDGL FQTPIYRNLL PSVGVQRQPL QELMLGYSDS NKDSGFLSSN
     WEIHQAQIAL QTLASSHGVA LRLFHGRGGS VSRGGGPAYQ AILAQPSGTL QGRIKITEQG
     EVLASKYGLP ELALYNLETV TTAVVQNSLV TNQLDATPSW NQLMSRVAKR SREHYRALVH
     DNPDLVAFFQ QVTPIEEISK LQISSRPARR KTGARDLSSL RAIPWVFGWT QSRFLLPSWF
     GVGTALAEEV NDDPEQLDLL RRLHQRWPFF RMLISKVEMT LSKVDLDLAH HYMSSLGNPE
     QRDAFEGIFK VIADEYGRTL KLVLEITGQS RLLGADQNLQ LSVDLRNRTI VPLGFLQVAL
     LRRLRDQNRQ PPMSESPGTP EDRRTYSRSE LLRGALLTLN GIAAGMRNTG
//