ID A0A0A6YCT1_9MICC Unreviewed; 921 AA.
AC A0A0A6YCT1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=GY22_07295 {ECO:0000313|EMBL:KHD97977.1};
OS Kocuria polaris.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=136273 {ECO:0000313|EMBL:KHD97977.1, ECO:0000313|Proteomes:UP000030466};
RN [1] {ECO:0000313|EMBL:KHD97977.1, ECO:0000313|Proteomes:UP000030466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 76or {ECO:0000313|EMBL:KHD97977.1,
RC ECO:0000313|Proteomes:UP000030466};
RX PubMed=12656171; DOI=10.1099/ijs.0.02336-0;
RA Reddy G.S., Prakash J.S., Prabahar V., Matsumoto G.I., Stackebrandt E.,
RA Shivaji S.;
RT "Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium
RT isolated from an Antarctic cyanobacterial mat sample.";
RL Int. J. Syst. Evol. Microbiol. 53:183-187(2003).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHD97977.1}.
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DR EMBL; JSUH01000005; KHD97977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6YCT1; -.
DR Proteomes; UP000030466; Unassembled WGS sequence.
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:KHD97977.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 579
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 921 AA; 101374 MW; 4B4DF210BBEF5B7E CRC64;
MIDAPLRADV RRITTLLGET LARQRGEELL ELVEQVRRLT KDAKDAKASG ADDAAGQVRD
LLGSLPLDRA TDLVRAFAHY FHLANAAEQV HRVRVLGRRP EDEGWLAAAV ADVAAEAGPD
ALREAVGSLD VRPVFTAHPT EASRRSVLTK IRHLSDILAR ETAEGSAARR SQDRRLAELI
ELLWQTDELR QNRPTPLDEA RNALYYLREV LTETMPVLLA DLEDQLSQHD VHLPAGPPPL
RFGSWIGGDR DGNPNVTPEM TRRVLQLQGQ AAVDIALSFL DVLVSRLSPS TAIVEVDPEL
RESVERDVAH LPGLDPRVLE LNAQEPYRLK LTCIKAKLIN TRRRFAEETV HEPGRDYRTT
AELVADLDVV ARSLRHHAGA LAADGSLAAA TRTIAGFGLG LATLDVREHA DAHHEAVGQL
LDRLGELDQP YADMDRGARA AVLAGELAGR RPLAPPGLST GAVHLDGDAD RTFAVFREIA
RAQETYGEEI VETYIVSMTR DADDILAPVI LAREAGLVDL TGEQDRATLG FAPLLETVGE
LRRSAEVIDE LLSDPAYRRV VAARGNIQEV MLGYSDSNKE SGVMTSRWEI HRTERRLRDV
AARHGVRLRL FHGRGGSVGR GGGPTHDAIL AQPSGVLAGE IKFTEQGEVI SDKFSLPALA
RENLELSLAA VLRATALHQD PRSTEEELDR WGEVMDVVSD AAFASYTGLV EDPDLPEYFL
SATPVEQLGA LNIGSRPAKR PSSDKGLSGL RAIPWVFGWT QSRQIVPGWF GVGSGLRAAR
EAGMEGDLRT MLERWHFFRS VISNVEMTVA KTDLEIAAHY VRALVPERIQ HVFEVIRREY
ELTLDELARL TGQAELLDGN PTLKQTLEVR DQYLDPISYL QVELLRRIRE QDAEGREVDE
GLQRALLITI NGVAAGLRNT G
//
