ID A0A088QW86_9CORY Unreviewed; 942 AA.
AC A0A088QW86;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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:AIN82026.1};
GN ORFNames=DR71_2194 {ECO:0000313|EMBL:AIN82026.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN82026.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN82026.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CP008913; AIN82026.1; -; Genomic_DNA.
DR RefSeq; WP_038628972.1; NZ_CP008913.1.
DR AlphaFoldDB; A0A088QW86; -.
DR STRING; 1487956.DR71_2194; -.
DR GeneID; 64051245; -.
DR KEGG; coa:DR71_2194; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR Proteomes; UP000029247; 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:AIN82026.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029247}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 603
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 942 AA; 105109 MW; 42231A347C0DBEA8 CRC64;
MNEQVHRDAD RNTASNEQSS STATAKQQDL LWEDIRHLGR ILGQVIREQE GDEVFNLVEN
ARRAAFELHR GDGDIEKLAG LFRDIDPAEA SPVIRAFTHF ALLANLAEDL HEELGIEASL
DAGDPPQDST LEATWQKLRD AKVSGSAIAD MMDHIEVVPV LTAHPTETRR RTVFDVQKHI
TAAMRRRHEI QAAPLNARTA DRLAEIDADI RRRILTLWQT ALIRMNRPDI RDEVEVGLRY
YQLSLLEAVP QINRDVVKHL RQLGGDKLQA NPTIRMGSWI GGDHDGNPYV TEETLRYASD
RAAGTILRHY FSQLHLLERE LSLSDRLTKV TVDLVALASR GHNDVLNRED EPYRRAVHGI
RGRVAATAVN FFDESIIEGD WSEFTPYDSA EDLLEELSII DDSLRSSHDD LIADHRLRDL
MDAVEVFGFH LYSIDIRQNS DSHEEILTEL FSAAGVVDNY AGLKEADKVE LLTKELQSSR
PLVSTSADLS EATARELGIM RAASRAVRKY GRDAVPHCII SMCTSVSDLL EPMILLKEVG
LIRPNGSQPT GSVDVIPLFE TIEDLQAGAD VLRAAWDIPV YRAYVSARGD LQEVMLGYSD
SNKDGGYFAA NWALYDAEVA IVAAAKDNDI RLRLFHGRGG TVGRGGGPSY EAILAQPSGA
VQGSVRVTEQ GEIISAKYGH PAAARRNLAA LVSATIESTL LDVDDLKNPA RAHEIMSEIS
DLSREAYSKL MHEDPGFIDF FTSSTPVDEI GSLNIGSRPT SRKQTQTISD LRAIPWVLSW
SQQRSMVPGW FGVGSALQEW IGEDEDGSRL AELRQLNEDW PFFNSVLSNM AQVMSKADLN
LARAYASLCE NKADGERIYS IIKAEFDLTL KMFLKVTGYK DLLEDNPLLR RSVDMRFPYL
MPLNIIQLEM LRRYRAGDNR DKVRRGIQLT MNGLATALRN SG
//