ID   D5URT4_TSUPD            Unreviewed;       921 AA.
AC   D5URT4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=Tpau_2536 {ECO:0000313|EMBL:ADG79139.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS   100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS   (Corynebacterium paurometabolum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG79139.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC   KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG79139.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC   KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R.,
RA   Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain (no.
RT   33).";
RL   Stand. Genomic Sci. 4:342-351(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, 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; CP001966; ADG79139.1; -; Genomic_DNA.
DR   RefSeq; WP_013127158.1; NC_014158.1.
DR   AlphaFoldDB; D5URT4; -.
DR   STRING; 521096.Tpau_2536; -.
DR   KEGG; tpr:Tpau_2536; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000001213; 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:ADG79139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213}.
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        583
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   921 AA;  101575 MW;  15A20D28394A927C CRC64;
     MTSEPARAAT EPLRDDIRLL GGILGDTVRE QAGERIFDLV ENARQESFRV RRSEIDREQL
     AAMFTDLPTA EAVPVIRALS HFALLANLAE DLHRERRRAI HVRAGEAPQA SSLAHTYTLL
     EDAGLDGDAV RAALRHALVV PVITAHPTET RRRTVFDTQH RITELMRYRD RTQLDPREEE
     QVQVNLRRQI LTLWDTALVR LERLRIQDEV VNGLRYFDAA FLEVMPQINH EIRTRLRELY
     PGTGLLSEPI LRPGSWIGGD RDGNPYVTGE VVTMASRRAA ATALEHYLRQ LLELEKELAL
     SLRLTTVSDE LLALAEWDTS PKQADEPYRR ALRWIRGRLS TTAADLLDEP LDAGIDIDAP
     RYGGPSELLA DLAVVDASLR TAGDGLIADA RLQDLREALN TFGFHLSGLD MRQNSDVHEE
     TISELFAWAG VHPDYASLDE SDRVRLLTDE LRLRRPLVGP GAEFTEQTAK ELGVLHAAAD
     AVANLGPGAV PNYIISMCTS VSDLLEAAVL LKEAGLLRPG DGSAADAVAT CSVNIVPLFE
     TIEDLQQGAA TMRAAFEVPV YRSLVDGKGG LQEIMLGYSD SNKDGGYLAA NWALYRAELD
     LVAMARDAGV TLRLFHGRGG TVGRGGGPSY DAILAQPPGA VRGTLRLTEQ GEIIAAKYAE
     PALATRNLES LLAATLESTL LDVEGLGDDA EEAYAVLDEL AALAREAYGD LVHRTDGFVE
     YFTTSTPVEE IGSLNIGSRP SSRKQTSKIS DLRAIPWVMA WSLSRVMLPG FYGTGAAIEK
     WIDGGPSRLE QLRALYRRWP FFQTVLSNMA QVLAKSDLGL AARYAELVPD AALRERVFGK
     IADEHRRTIE MYYAIAETDD LLADNPALKR SVFNRFPYLE PLNHLQVELL RRYRAGDTDP
     QVQRGILLTM NGLATALRNS G
//