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
//