ID S5SRV5_9CORY Unreviewed; 914 AA.
AC S5SRV5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=B841_01370 {ECO:0000313|EMBL:AGS33757.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS33757.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS33757.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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|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; CP003924; AGS33757.1; -; Genomic_DNA.
DR RefSeq; WP_020933692.1; NC_021915.1.
DR AlphaFoldDB; S5SRV5; -.
DR STRING; 1224163.B841_01370; -.
DR KEGG; cmd:B841_01370; -.
DR PATRIC; fig|1224163.3.peg.277; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000015388; 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; 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.
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:AGS33757.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015388}.
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 577
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 914 AA; 101896 MW; 975BC6DAB1F94C79 CRC64;
MSDQVRDDIR LLGRILGRVI AEQEGEDIYE LVEDTRRRAF AVARGEEDPE SLLAIFRTVD
EHKINLVARS FSYFALMANI AEDLDDETSL AQREDAGEAA PAASLDGVLA KLREADSVTP
GDVAQMLRTA QVSPVLTAHP TETRRRTVFD VQKRIIHLLR ERHGLINRPE TPRRRNRLSE
IEREIHLRMT LLWQTALIRI ARPQIEDEVN VGLRYFKLSL LEEVPAINRD VLAGLREVFG
TEVPSTQIVR TGSWIGGDHD GNPFVTGETL TYATRKAADT VLGHYVEELG ELERELSLSD
RYSDSSAELQ ELAARGRNDV PSRVDEPYRR AIHGVHGRIR ATRAVVAGDT AADGHEPYAS
PQEFLADLDV IDRSLREFSD AIIADDRLLR IRSAVESFGF HLNALDLRQN SESFEAVLDE
LFAAAGVVRG YAGLNEEEKR KVLTEELASA RPLTFSWAEP FSEPTERELG IFRAAADAVN
LLGPEVIPHC IVSMTGTVSD VLEPMVLLKE VGLINFDAAQ GRLVGSVDVA PLFETIDDLK
AGAAILEELW DVPLYRQYLR GRGDLQEVVL GYSDSNKDGG YLSANWALYD AELAVVEACA
ARGINLRFSH GRGGAVGRGG GPTYDAILAQ PKGAVQGSIR ITEQGEVISA RYGQNSTARR
HLEAFVAGTL EASLLDTESL QESERAYGIM REIAELAGEK YADLIRRDPG FIDYFTQSTP
LHEIGDLNMG SRPTARKQTS SVADLRAIPW VLSWSQSRVN LPGWFGVGTG VTRWAGDDEA
RWQDLRTLYR AWPFFRSVLD NMAQVMGKAS MDLAQMYSRL VDDPEVSRRI FQTISDEYEL
TREIFRRITG HESLMAGNER LERSVYRRYP YLLPLNAIQV ELLRRYRAGD DSFLVSKTIQ
VTMNGLATGL RTSG
//