ID   K0ESY9_NOCB7            Unreviewed;       923 AA.
AC   K0ESY9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   ORFNames=O3I_013180 {ECO:0000313|EMBL:AFU00597.1};
OS   Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFU00597.1, ECO:0000313|Proteomes:UP000006304};
RN   [1] {ECO:0000313|EMBL:AFU00597.1, ECO:0000313|Proteomes:UP000006304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700358 {ECO:0000313|Proteomes:UP000006304};
RX   PubMed=22535940; DOI=10.1128/JB.00210-12;
RA   Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R., Perez-Maya A.A.,
RA   Ocampo-Candiani J.;
RT   "Complete genome sequence of Nocardia brasiliensis HUJEG-1.";
RL   J. Bacteriol. 194:2761-2762(2012).
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; CP003876; AFU00597.1; -; Genomic_DNA.
DR   RefSeq; WP_014983452.1; NC_018681.1.
DR   AlphaFoldDB; K0ESY9; -.
DR   STRING; 1133849.O3I_013180; -.
DR   KEGG; nbr:O3I_013180; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000006304; 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:AFU00597.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006304}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        585
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   923 AA;  101363 MW;  AA4CC828370A2740 CRC64;
     MGESTSEAQQ DAIRPLRDDI RFLGGVLGDT IRDHEGPEVF DLIEQVRIEA FRVRRAEVDR
     SAVAEMLDGV DIAVALPLIR AFSYFVLLAN LAEDIQRDRR RAAHEAAGEP PQDSSLAATY
     RKLDAAALDG AEVADLLADA LVSPVITAHP TETRRRTVFD AQTRITELMR LRQRYTETER
     QRADFEQQIR RQVLSLWRTA LIRLARLRIQ DEISVGLRYY DITLFDVIPA INAEVRAALR
     SRWPGVELLP RPILRPGSWI GGDRDGNPYV TADVVRQAGQ QAATVAFSRY LRDLVELEKV
     LALSVRLVPV TPAVAALAEA GYPEPATHAD EPYRRALHRI RGRLTATAVR ALGEVPADGL
     DVGAEPYRTP QDVLDDLDAV DASLRASGDD LLADHRLAAL RHAIETFGFH LQGLDMRQNS
     EIHEQVVAEL LAWAGVHADY ASLSEPERVE LLAAELRTRR PLLGPHARLS ELARKEVDIV
     CAARDVVSTF GSEAVPNYII SMCTSVSDML EAALLLKEGG LLDPGEPDGP PSCAVGIVPL
     FETIEDLAAG AATLSAALDV PVYRDLVAAR GMRQEVMLGY SDSNKDGGYL AANWALYRAE
     LELVEVARKS GIRLRLFHGR GGTVGRGGGR SYDAILAQPA GAVRGALRLT EQGEVIAAKY
     AEPGAAHRNL ESLIAGTLES TLLDVEGLGP DAEPSYELMD ELAERARAAY ARLVHDTPGF
     VEYFRQSTPV AEVGDLNIGS RPASRKPTNS VADLRAIPWV MSWSQARVML PGWYGTGTAL
     EEWIGDDPQR LATLTDLYER WPFFRTVLSN LAQVLAKSDL AIAARYAELV DDVALREQIF
     GMIKDEHART IRMHAAVTGN DHLLADNPSL AESIHNRFPY LEPLNQMQVQ LLRRLRAGDD
     SELVKRGILL TMNGLATALR NSG
//