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
//