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Database: UniProt
Entry: F4XYJ5_9CYAN
LinkDB: F4XYJ5_9CYAN
Original site: F4XYJ5_9CYAN 
ID   F4XYJ5_9CYAN            Unreviewed;      1072 AA.
AC   F4XYJ5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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   ORFNames=LYNGBM3L_51900 {ECO:0000313|EMBL:EGJ30408.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ30408.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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; GL890954; EGJ30408.1; -; Genomic_DNA.
DR   RefSeq; WP_008188014.1; NZ_MKZR01000001.1.
DR   AlphaFoldDB; F4XYJ5; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000003959; Unassembled WGS sequence.
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; 2.
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:EGJ30408.1}.
FT   REGION          110..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        719
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1072 AA;  122236 MW;  588E92FB091E5989 CRC64;
     MSFLPSPSNQ DSTFPATSDL FLRHRLKIVE DLWESVLLSE CGQELVDLLK QLRELCSPEG
     QATEDPKSSV ADLIQQLDLN EAIRASRAFA LYFQLINIVE QHYEQRNQQL SRRRSYRKST
     EPELSPFSQG ILTKNGNSSF STVVTVEQEV DIGNDVTQPG GAVTNVIEKS QQENQGSQRK
     LGLLDWLFPH LHKQNVPPGQ IQRLIDNLDI RLVFTAHPTE IVRRTIRGKQ RRMAKILEQL
     DQAEQTYGTL GITSSWEVTE CSQKLMEEIR LWWRTDELHQ FKPGVLDEVD YTLHYFQEVL
     FDTIPQLYSR FKQALKGSFP WLNPPAKNFC HFGSWVGSDR DGNPFVTPQI TWQTACYQRD
     LVLGKYIGEV RNLTELLSLS LHWCDVLPEL LDSLEQDRSQ LPEVYEQLAI RYRQEPYRLK
     LTYVKQKLEN TRERNQQLAN GMPVPDEMAN GKSWSFYRSG EEFLAELKLI ESNLLETGLN
     CRELDNLICQ VEIYGFYLAH LDIRQESSRH SEALSEIAEY LQVLPKPYNL LSESEASLWL
     TAELRTRRPL IPTELPFSEK TCETIETFRM VRQLQQEFGP QICQTYIISM SHTASDLLEV
     LLLAKEAGLY DPATGKSTIR VVPLFETVED LKRAPAVMKS LFELPLYRAS LAGGYQQMQV
     SPNNRQLNNL PYSNAKAEQP NNPDLKAVGH AARTATLREQ GLTSPNLQEV MLGYSDSNKD
     SGFLSSNWEI HKAQKALEHM AEEYGIVLRI FHGRGGSVGR GGGPSYEAIL AQPGRSINGR
     IKITEQGEVL ASRYSLPGLA LYHLETIATA VMQASLLNNG FDDIQPWNEI MEELAQISRS
     HYRALIHDQP DLVDFFHQVT PIQEISQLQI SSRPARRKSG KKDLSSLRAI PWVFSWTQSR
     FLLPSWYGVG TALQSFVDQA PEENINLLRC FYSKWPFFKM VISKVEMTLA KVDLQIAHHY
     VKELSNPEDL ERFEHLFEQI AKEFNLTRNL VLTITGHQTL LDGDPNLQRS VHLRNGTIVP
     LGFLQVSLLK RLRQHSNQVT LGVVQSRYSK GELLRGALLT INGIAAGMRN TG
//
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