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Database: UniProt/TrEMBL
Entry: Q0ICY4_SYNS3
LinkDB: Q0ICY4_SYNS3
Original site: Q0ICY4_SYNS3 
ID   Q0ICY4_SYNS3            Unreviewed;      1001 AA.
AC   Q0ICY4;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:ABI46533.1};
GN   OrderedLocusNames=sync_0460 {ECO:0000313|EMBL:ABI46533.1};
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI46533.1, ECO:0000313|Proteomes:UP000001961};
RN   [1] {ECO:0000313|EMBL:ABI46533.1, ECO:0000313|Proteomes:UP000001961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311 {ECO:0000313|EMBL:ABI46533.1,
RC   ECO:0000313|Proteomes:UP000001961};
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP000435; ABI46533.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0ICY4; -.
DR   STRING; 64471.sync_0460; -.
DR   KEGG; syg:sync_0460; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001961; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ABI46533.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001961}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..976
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        643
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1001 AA;  112840 MW;  34237888CB62A6B2 CRC64;
     MIPSDSGFPS MHSSSALIPE STQPRADGNE AGGGQLLQQR LALVEDLWRT VLRSECPPEQ
     AEQLLRMKQL SDPVLPGEHP AGTDALIDLI KGMDLAEAIA AARAFSLYFQ LVNILEQRIE
     EDTYLESINR SQDQAEQFDP FAPPLATQTE PATFRELFER LRRLNVPPAQ LEALLQELDI
     RLVFTAHPTE IVRHTVRHKQ RRVASLLQQL ETQPPTPSGA TDSVRLQLEE EIRLWWRTDE
     LHQFKPSVLD EVDYALHYFQ QVLFNAMPQL RRRIVASLAA SYPDVRVPSS SFCTFGSWVG
     SDRDGNPSVT TEITWRTACY QRQLMLDRYI SAVQHLRNQL SISMQWSQVS PPLLESLEMD
     RLRFPDVYEE RATRYRLEPY RLKLSFVLER LRLTQLRNQQ LADAGWRTPP EGLPSFTPGN
     APGDALHYGS IAEFRSELEL IRTSLVNTDL SCEPLDTLLT QVHIFGFSLA GLDIRQESTR
     HSDALDELSR YINPDRAYGA MDEAERVAWL MEELQTRRPL IPPAVSWSAA TAETVDVFRM
     LHRLQDEFGS RICGTYVISM SHSVSDLLEV LLLAKEAGLV DPSARHADLL VVPLFETVED
     LQRAPEVMEH LFQTPLYRDL LPKVGTQGLL LQELMLGYSD SNKDSGFLSS NWEIHQAQIA
     LQDLASRQGI ALRLFHGRGG SVGRGGGPAY QAILAQPSGT LQGRIKITEQ GEVLASKYSL
     PELALYNLET VTTAVIQNSL VTNQLDATPS WNKLMSRVAK SSRRNYRALV HDNPDLVAFF
     QQVTPIEEIS KLQISSRPAR RKTGTRDLSS LRAIPWVFGW TQSRFLLPSW FGVGSALSEE
     LEADPDQLTL LRTLHQRWPF FRMLISKVEM TLSKVDLDLA RHYVTSLGSA EHHEAFEKIY
     ATVAEEYART KELVLAITGQ ERLLDADPAL QLSVDLRNRT IVPLGFLQVA LLRRLRDQNR
     QPPMSESPSS DGDGRTYSRS ELLRGALLTI NGIAAGMRNT G
//
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