ID   M1MXS4_9CORY            Unreviewed;       921 AA.
AC   M1MXS4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=A605_07660 {ECO:0000313|EMBL:AGF72534.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72534.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF72534.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72534.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA   Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT   type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(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; CP003697; AGF72534.1; -; Genomic_DNA.
DR   RefSeq; WP_015400953.1; NZ_JIAJ01000001.1.
DR   AlphaFoldDB; M1MXS4; -.
DR   STRING; 1121362.A605_07660; -.
DR   KEGG; chn:A605_07660; -.
DR   PATRIC; fig|1121362.3.peg.1547; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011723; 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:AGF72534.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011723}.
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   921 AA;  101955 MW;  91ABC160BCA6D9D4 CRC64;
     MTPADHLQED IRYLGRVLGR VIAEQEGEEV FDLVEHARQL AFGIAKGDTG LEALVELFRN
     IEPARATPVI RAFSHFALMA NLAEDLHDDF TRERLLDAGG PAPDSTLETT WAKLAGAGVD
     AATVAEALDG ALVAPVLTAH PTETRRRTVF DAQRHITEQM TVRHRLLEAP HTARTDSQLE
     EVDRQIRRRL TILWQTALIR MARPRIEDEI EVGLRYYKLS LLEEIPALNR AVDDRLRADF
     GQGVPTRALV RPGSWIGGDH DGNPFVTAAT LDYATRRAAQ TVLKHYETQL LALEHELSLS
     DRMTSVTVDL VALAKRGLND VPSRVDEPYR RAIRGIRGRL LATTATLIGE DAVEGSWHRV
     HEPYSGPGEF DADLAVIDES LRRSHDEIIA DDRLATIRAA VAGFGFHLYS LDLRQNSESF
     EAILAEVFAA AGVHDDYASL GEEERIDLLT RELRTPRPLV PRGRRGFSEP TQRELDLFEQ
     AATSVERFGM EMIPHLIISM ATSVSDILEP MVLLKEVGLL HADGERPTGS VDVIPLFETI
     DDLAAGAGIL RELWALPLYR AYLAQRGDVQ EVMLGYSDSN KDGGYLAANW ALYDAETQIV
     AAGRDHGVRL RLFHGRGGTV GRGGGPSYEA ILAQPKGAVD GSVRITEQGE IISAKYGSGH
     TARRNLEALV SATLEASLLD VDELVDRERA TGIMTEIARL SRARYSRLVH EDPGFIPYFT
     QSTPLDEIGA LNIGSRPTSR KQTNSVADLR AIPWVLAWSQ SRVMLPGWFG VGTALAEWIG
     EGDDAEDRCA ELRHLYETWP FFTSVMSNMA QVMSKAGMEL AGLYAGLVDD REVAGRIRGI
     ISEEFRLTRE MFTKVTGSED LLADNPMLAR SVRRRFPYLL PLNIIQVELL RRHRAGDERD
     AVSRGIRLTM NGLATALRNS G
//