ID   E8RL05_ASTEC            Unreviewed;       890 AA.
AC   E8RL05;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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   OrderedLocusNames=Astex_1955 {ECO:0000313|EMBL:ADU13618.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS   NCIMB 9791 / VKM B-1370 / CB 48).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU13618.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC   CB 48 {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Brun Y.V., Woyke T.;
RT   "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; CP002395; ADU13618.1; -; Genomic_DNA.
DR   RefSeq; WP_013479448.1; NC_014816.1.
DR   AlphaFoldDB; E8RL05; -.
DR   STRING; 573065.Astex_1955; -.
DR   KEGG; aex:Astex_1955; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001492; Chromosome 1.
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:ADU13618.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001492}.
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        550
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   890 AA;  98725 MW;  F2F59EE11FD9D2D0 CRC64;
     MTDAMIDHVK QNTAMLEGFL TDAVNSFGRG TVLSKIEALR ADNADVDDLS ESEAAHAARV
     LTCLSTLTVL SEDVANLKRV ETFPGTQEAI TLANAVQQAR AKGHSQAEIE ETLNGILASP
     VFTAHPTEMR RASVVEREYD ITQFLSAYER TTRASERKAL EEDLFRAVAL LFNTRLNRPE
     RITVADEIQN SLGAVRRAIL PALVELYGDW NREIELEGEL PNVLKLGSWI GGDRDGHPHV
     DDTTMNYAFH NQAKLVLDFY FQQLDKLDIE LTLSEELAPV TDALLELARK SSDTNVHRVD
     EPYRRALTFI KTRLASTWQA ILKLPHPLAS PLAGAYETSE NFVRDLLIIR DSLIEYGGKR
     LVGRTLKSTI QIARSCGFHL LSLDMRQNSA VHERVIAELF AQSSELLDYS SLSENERVSA
     LVAELTNDRL LRWPFAKYSD ETRRELRIID AAAEVIRTFG PDAIGAYVVS MAKSVSDILE
     PLVLLKQAGL VYGGPSPHTM IRVSPLFETI EDLEAAPDIM KRWLGLPAMR SLMGRPAVQE
     VMLGYSDSNK DGGYTASRWS LHKASSAIKA VCNQKGVALR LFHGRGGSVG RGGGPSFNAI
     MAQPEGTVGG QIRVTEQGEM IARKFGNKTT AGKTLDSFSA AVFLASLPVK ERDAHHIKES
     EAEAKYGPLM NQLCKASFDA YRALVYDDPH FLDFFRSVTP ISEISDLKIG SRPASRTKSG
     KIEDLRAIPW VFSWSQSRMV LPGFYGFNAA VKALGVDDQT LIDMCNEWDF FEVFLANMEM
     ALAKSDMEMA SLYAGMASDP VEAQRIFATI RQEHEEMTAL AKRIRKAGTL LSTHEQLRGS
     IERSHALLQT LNRMQVKLLK KRREGNKHKL VKLAMQLTVN GIASALRNTG
//