ID   D5UGP1_CELFN            Unreviewed;       891 AA.
AC   D5UGP1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Cfla_2248 {ECO:0000313|EMBL:ADG75139.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75139.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG75139.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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; Evidence={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; CP001964; ADG75139.1; -; Genomic_DNA.
DR   RefSeq; WP_013117473.1; NC_014151.1.
DR   AlphaFoldDB; D5UGP1; -.
DR   STRING; 446466.Cfla_2248; -.
DR   KEGG; cfl:Cfla_2248; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000849; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:ADG75139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849}.
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   891 AA;  97456 MW;  62946A73A317C7D0 CRC64;
     MNQAEIGPDV PRGVVSHEVP ELLRNDVRLL GELLGRVLRE AGGEDLLADV ERLRELAIAS
     HSEPNGHALA EAEQLVAGFG HERAEQVARA FTCYFHLANL AEEYHRVRVL RDRESRLSPH
     ELAPDDSLPA AYQQLVDEIG PDAARRRLHE LEFRPVFTAH PTEARRRAVS RAIRRIAELV
     AERDTLHIGG TTLAENERRL LAEIDTLWRT SPLRAEKPTV LDEVATVLSI FDATLADVLP
     TVYRRLDDWL LEDEAGTTAP TVAPFARLGS WIGGDRDGNP NVTAEVTRAA AAMASEHALD
     ALLVSARRTA DGLTLDAAGT PPSTELSALW QRQRSLSDAI TSRIADAAPN EPHRRALLGI
     VERVAATRRR DADLAYAGAD ELEADLLIVQ ESLRAAGAHR AAFGDLQRLV WQVQTFGFHL
     AELEVRQHSQ VHEAALADIE AHGVDGELQP MTVEVLDTFR ALGTVQRRLG VKAARRYIVS
     FTQSPEHLAA VYTLADLAFG GPEHAPVIDA IPLFETFADL QNSVDILEAA LEHPRVQERL
     AANGRRVEVM LGYSDSSKDV GPLSATLALD DAQRRIAEWA RRHDIVLTLF HGRGGALGRG
     GGPANRAVLA QPPGSVDGRF KLTEQGEVIF ARYGDPDIAA RHIEQVTAAT LLADAPSVVQ
     RNDTAAARFA DLAARLDVAS REHFHRLVRA DGFPAWFAQV TPLEELGLLP IGSRPARRGL
     SVSSLDDLRA IPWVFSWSQA RINLAGWYGL GTALEAVGDA EALRVAYAEW PLFATIIDNV
     EMSLAKTDER IAARYLALGD RDDLAQLVLD ELRRTRTWVL AVTGSTGVLS RRRILGRAVQ
     LRSPYVDALS LLQLRALRGL RTGEPNESAD DLRRLLLLTV NGVAAGLQNT G
//