ID   B4R835_PHEZH            Unreviewed;       898 AA.
AC   B4R835;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
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:ACG77568.1};
GN   OrderedLocusNames=PHZ_c1154 {ECO:0000313|EMBL:ACG77568.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77568.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG77568.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG77568.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; Evidence={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; CP000747; ACG77568.1; -; Genomic_DNA.
DR   RefSeq; WP_012521714.1; NC_011144.1.
DR   AlphaFoldDB; B4R835; -.
DR   STRING; 450851.PHZ_c1154; -.
DR   KEGG; pzu:PHZ_c1154; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001868; 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; 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.
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|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ACG77568.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   898 AA;  98097 MW;  6488C5163E90C13D CRC64;
     MTQSVPDQLR AAVRFLGRVL GDVIRAQDGV AVFNQIEDIR QASVGFHREG TPEAARLMAE
     RLGSLSLEDT VRFAHSFACF LQITNIAEDQ IQRRRIRAGE ARPDTLAGAV RALAADGVER
     KEVEDLLAGA LIAPVITAHP SEVRRKSVLD RQSAIARGLE AFDRARTDAE REAAEQELVR
     EVSIFWRTRL LRHVKIAVGD EIENAVSYFE RSFLAALPRL YARWRHVLGQ DEALASFLRV
     GSWVGGDRDG NPFVTAQVMR QALARQSRAA LRLYLDQVHA LGAELSISSD LAGVTPELQA
     LADKAHDASP HRTDEPYRRA LTGVYARLAA TYPLLTGEAP PRPASTPGEP YEDPQTLRAD
     LQTVLDSLLR MHGEAFADGP LPDLIRAVDV FGFHLATLDM RQNSAVHARV AAELLRTAGV
     CADYEALDEA GRCQLLLSEL RHGRLLASPF ATYSEETARE LEILATAAEI KRRYGPDSIR
     AYIVSNTTSV SDLLEVYLLL KEVGLFRPGA PPTAEILAEP LFETIEDLRA APKTMARYLA
     LPQIHDLLAG HGLQEVMIGY SDSNKDGSYL TSTWELHKTS RALASVVGGA GLRLQLFHGR
     GGAVGRGGGS SFEALVAQPR GTVGGRIRIT EQGEVVANKY ADPELAGQSL ETLTAGVVLA
     SLRRHASEDL AAPQTKAMDA LARHAMQAYR SLVYETPGFV DYFFAATPIA EIADLNIGSR
     PTSRQASRSI QGLRAIPWVF SWSQSRAMLP GWYGFGSAVA NGGVPMAQLR ELFESWPFFA
     TTLANMEMVL AKGDLAIAGR YAGLVEDQAL AETVFGQIRA EWERTTEALL EITGQSALLE
     HNPDLAAVIR SRLPYIDPLN HLQIELIRRR RSGDDQEAVR QGIHLTINGV AAGLRNTG
//