ID   K4KMC3_SIMAS            Unreviewed;       870 AA.
AC   K4KMC3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   OrderedLocusNames=M5M_11040 {ECO:0000313|EMBL:AFU99385.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU99385.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFU99385.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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, ECO:0000256|HAMAP-
CC         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; CP003746; AFU99385.1; -; Genomic_DNA.
DR   RefSeq; WP_015047549.1; NZ_ATUQ01000004.1.
DR   AlphaFoldDB; K4KMC3; -.
DR   STRING; 1117647.M5M_11040; -.
DR   KEGG; saga:M5M_11040; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000466; 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:AFU99385.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466}.
FT   ACT_SITE        134
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        535
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   870 AA;  97170 MW;  0C874E9879902F29 CRC64;
     MSALRNQVKA LGSLLGQTIA DHEGQDCLDL IETIRLQSKA IDAGDQAALA DLTGKISAAD
     DKTLLTIARA FSQFLNLANI AEQIYTVSDE AKTLIDRPDP FASLRSQFEN QRWSAEAFTR
     AAEKLHMDLV LTAHPTEVTR RTLIHKYRQI FDQLRRGDDV DMTRIQELIS QDWMTNSIRR
     IRPTPVDEAS WGLAVIEDSL WEAVPRFLRE LDAQSEQITG KPLAPQITPL RMSSWMGGDR
     DGNPFVTAKL TRQVIAMSRA KAAELYARDL EQLSMELSMM DASDDLWALL PEQHKDSEQP
     YRELIRPVRK LLAHTREQMD ELYRTGSRSD NQPVLESVEQ LLTPLYQCYD SLMRCGLTRI
     ARGYLLDTIR RIQCFGVGLI RLDIRQHSER HNDVMAEITR ALGVGDYLSW SETERQAFLR
     AELDNPRPLL PIHFAPSAEV QEVLDTVQVI AETPAEMMAI YIISMASQPS DVLLVELLQK
     ACGVKKPLPV APLFETLDDL DNAEGVMRDL MAMPGYKARA KGRQYVMIGY SDSAKDAGVL
     AASWAQYRAQ DALIKLHTAE GMDLTLFHGR GGTIGRGGGP AHAAILSQPP GSVNGGLRVT
     EQGETIRYKF GLPKLAVRSL SLYASAILEA LLAPPPEPKA EWRALLDSMA DTACKTYRYY
     IREEPDFVRY FRQATPEQEL GQLPLGSRPA KRKAEGGIES LRAIPWIFAW SQNRLVLPSW
     LGFGTALKQA VDNGSADLLK DMQANWPFMR SRLAMMEMVY SKSDSHIASL YDARLVDDSL
     KGLGQALRNQ LSEDTATLLN FLGQQALLEN DAWGAQSLDV REIYLVPLHL LQIELLARVR
     AKQDVDQVSD CNRALMVAMA GIAAGMRNTG
//