ID   F2I8N9_AERUA            Unreviewed;       903 AA.
AC   F2I8N9; A0A9Q4DCA4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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:AEA01718.1};
GN   OrderedLocusNames=HMPREF9243_1989 {ECO:0000313|EMBL:AEA01718.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA01718.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002512; AEA01718.1; -; Genomic_DNA.
DR   RefSeq; WP_013669937.1; NZ_JAOTMI010000016.1.
DR   AlphaFoldDB; F2I8N9; -.
DR   STRING; 866775.HMPREF9243_1989; -.
DR   KEGG; aur:HMPREF9243_1989; -.
DR   PATRIC; fig|866775.3.peg.1882; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000008129; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:AEA01718.1};
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:AEA01718.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008129};
KW   Transferase {ECO:0000313|EMBL:AEA01718.1}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        566
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   903 AA;  103123 MW;  0D2023A7C1C5FD87 CRC64;
     MPVKKLEANI TQSMVKEEVH VLKEILDDTT HKMVGDQVFE MIQGLVDLSM KEDYKQLESV
     VAQLSNDEMV VVSRYFSILP LLINISEDVD FAYEINYQNN TDQDYLGKLA LTIDRVSQSD
     QAKEILEHVN VVPVLTAHPT QVQRKTILEL TNQIHHLLRK YHDVKAGVVN RDKWYTDLRR
     YVEIIMQTDI IREKKLTVRN EITNVTAYYN NSLIRAITKL SRQYRHLAAQ KGIELDQAKP
     ITMGMWIGGD RDGNPYVTAE TLLLSATTQS EVILNYYIDK VHKLYRNFSL STTLVDISPA
     MEALAAKSND KSIYRENEPY RRAFHYIKAK LEQNLVEVKN GLKRDDQAPT PSYQNAEAFK
     ADLLVIKESL LAHGEDALLT GDFNELVEAI DIFGFYLATI DMRQDSSVNE ACVAELLKSA
     KIVDDYSSLS EPEKVKVLLK ELLEDPRPLS SAHSEKSELL EKELKIFKTA RFLKDQLGDQ
     VIKQHIISHT ESVSDMFELA IMLKEVGLVD PKQARVQIVP LFETIEDLEN AQGIMEEFLS
     YDLVQNWIKA NHGYQEVMLG YSDSNKDGGY LSSVWTLYKV QQELTQLGED HGIKITFIHG
     RGGTVGRGGG PSYEAVTSQP FGSIKDRIRL TEQGEIIENK YGNQDVAYYN LEMLVSAAIS
     RIVPGSVDKK ADVEDFYQDM DDIVHYSNGV YRHLVFDTPE FYDYFFEATP IKEVSSLNIG
     SRPAARKTIT EISGLRAIPW VFSWSQTRIM FPGWYGVGSA FKHFIDQDAG NLEKLQAMYQ
     SWPFFHSLLS NVDMVLSKSN MNIAEQYAQL AESEEVRAVF TTIRDEWQLT KDILLAIENH
     NEFLATNPSL RASLDYRLPY FNVLNYIQIE LIKRLRHNEL DEDYEKLIHT TINGIATGLR
     NSG
//