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Entry: A0A0F6TD32_9CORY
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ID   A0A0F6TD32_9CORY        Unreviewed;       922 AA.
AC   A0A0F6TD32;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ECO:0000313|EMBL:AKE41281.1};
GN   ORFNames=UL82_05530 {ECO:0000313|EMBL:AKE41281.1};
OS   Corynebacterium kutscheri.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE41281.1, ECO:0000313|Proteomes:UP000033457};
RN   [1] {ECO:0000313|EMBL:AKE41281.1, ECO:0000313|Proteomes:UP000033457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE41281.1,
RC   ECO:0000313|Proteomes:UP000033457};
RX   PubMed=26021937;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT   Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT   DNA.";
RL   Genome Announc. 3:e00571-15(2015).
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,
CC         ECO:0000256|HAMAP-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; CP011312; AKE41281.1; -; Genomic_DNA.
DR   RefSeq; WP_046439483.1; NZ_LR134407.1.
DR   AlphaFoldDB; A0A0F6TD32; -.
DR   STRING; 35755.UL82_05530; -.
DR   KEGG; cku:UL82_05530; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000033457; 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:AKE41281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033457}.
FT   ACT_SITE        141
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   922 AA;  103634 MW;  AE2A3EA186650568 CRC64;
     MTEKVEFTVL EDILYLAEIL GTVIATEISE ESVELIKKTR VLSFEIASGQ ADMQELVTLL
     ENTKVTDRIH IVRAFSHFAL LANVVEDVHD ARNAIIAAEN GEPAPDSTLE ATWTKLKKEV
     ASHQLKDVID RAEVAPVLTA HPTETRRRTV FDVQYHISEL LKRRHSTLAF PNALSKSRLK
     EIDQQVLRWL TILWQTALIR IARPRIEDEV EVGLRYYRLS LLEAIPEINR SINRSLVEQF
     NESPSENAVI KPGSWIGGDH DGNPYVTANT LRYATRRAGE TVLKYYVTQL HNLEHELSMS
     DRYTPISKEL IALADQGHND IPSRIDESYR RAVHGIRGRV LATLTDRIGS DSAEGSWHEI
     FKPYSCPEEL ADDLRIIDDS LRAAHDEVIA DEHLALIRSA VASFGFHLYS MDLRQNSESF
     EDTIHEVFQR AGVCSNYRDL NETDKRELLL AELVSPRPLL RTNAEPFSEP TQRELDLFAE
     AKRAVDSFGY RMIPHLVISM ASSVSDIFEP MVLLKEYGLL EVKDGNLFGH IDISPLFETI
     EDLQAGAAIL EELWQIPIYR KYLHSRNNVQ EVMLGYSDSN KDGGYFAANW ALYASEVELV
     KVGRKHNVSL RLFHGRGGTV GRGGGPSYEA ILAQPNGAVD ATMRVTEQGE IISAKYGSKD
     TALSNLEALV SATIEATLLE TDQLKDSREE AYEIMADIAA RSQKAYAQLV HEDPGFIQYF
     TESTPLAEIG SLNIGSRPSS RKQTESIDDL RAIPWVLSWS QCRVMLPGWY GVGSAISSWI
     AEGDRSSRIA QLRELKKTWP FFDSVLSNMA QVMSKAEMQL AEFYSQLVSD KQVGQRIYAA
     IAEEFDLTAQ ILAEITGDEL LADNPRLARS VRSRFPYLFP LNVVQLTFLK EYREMEDAEN
     SLVAQGIQLT MNGLSTALRN SG
//
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