ID   Q0RT35_FRAAA            Unreviewed;       978 AA.
AC   Q0RT35;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-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=argE {ECO:0000313|EMBL:CAJ59268.1};
GN   Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=FRAAL0594 {ECO:0000313|EMBL:CAJ59268.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59268.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ59268.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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, ECO:0000256|HAMAP-
CC         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}.
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; CT573213; CAJ59268.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RT35; -.
DR   STRING; 326424.FRAAL0594; -.
DR   KEGG; fal:FRAAL0594; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000000657; 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:CAJ59268.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        639
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   978 AA;  105144 MW;  4319176AE9A39A48 CRC64;
     MSGISANPGR PIRAKAEPGR PRRTADPGEP RRTTGGGVTT ERSASTTLDE LAPDPGAFAG
     GVSSDARHAA VRAGVRRLGD LLGQALTRHE GAATLALVEQ VRALARRPDN GAELGRLLAT
     VDDRTAIVLA RAFTAYFQLA NITEQLHRSR ELSDRAKGPL TETFDRMAAA LDAGTLDRSL
     AESIARRLEL RPVFTAHPTE ASRRSVLDTL RRIADLLDAD SPDGAVPAAD RDRTQRRLAE
     MVDVLWQTDE LRVERPKPAD EARSAAYYLE LIATEVLPDL LEELDLALAR VGLTLPAGAH
     PVRFGSWAGG DRDGNPNVTP AVTLEVLTLQ HEFGIRLLTA SVERLIQELT ASTRVVGVGD
     ELLSSLAADR EALPEVHDRY IRLNAEEPYR LKCSYILARL AGTRERLAAG APHVPGRDYG
     GVAEILDDLE VMRASLNAGD GSLVADGPLL RVIRTARAMG LSLATLDIRE HADKHHAALA
     AVYDQVGELD VPYAQLDRPA RRTLLSAELA RRRPLLGAVP PPLPPAVLGT LELMRTVREA
     LDRFGGDVIE SYIVSMTRDV DDILAVVVLA REAGLVGLGF ADRPAWARIG FVPLFETVAE
     LRAAGSLLDG MLSDPSYRSL VRARADVQEV MLGYSDSSKD AGITASQWEI HKAQRELRDV
     ARRHGVVLRL FHGRGGSVGR GGGPSGEAIM AQPFGTLDGS IKVTEQGEVI SDKYTLPQLA
     RHNLEITLAA VVEASILHRS SRLSPTVLAG WNETMQAVAD SARVTYQAFV GDPALVPFFL
     AATPVEELGN LNIGSRPSRR PGGTGGLADL RAIPWVFGWT QSRIILPGWF GVGTGLAAAR
     AAGAGDTLAE MYRSWHFFRT FLGNVQMTLA KSDLTIAQRY VSTLVGDDGG TIFETIRAEH
     ARTVAEVLTV TGQAELLENA PTLRHTLEVR DAYLAPLHAL QVSLLARARA AGEGADPLLR
     RALLLTINGI AAGLRNTG
//