ID   E5ANG6_MYCRK            Unreviewed;      1004 AA.
AC   E5ANG6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=RBRH_03119 {ECO:0000313|EMBL:CBW74148.1};
OS   Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
OS   (Paraburkholderia rhizoxinica).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Mycetohabitans.
OX   NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW74148.1, ECO:0000313|Proteomes:UP000007437};
RN   [1] {ECO:0000313|EMBL:CBW74148.1, ECO:0000313|Proteomes:UP000007437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19002 / CIP 109453 / HKI 454
RC   {ECO:0000313|Proteomes:UP000007437};
RX   PubMed=21131495; DOI=10.1128/JB.01318-10;
RA   Lackner G., Moebius N., Partida-Martinez L., Hertweck C.;
RT   "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont of
RT   Rhizopus microsporus.";
RL   J. Bacteriol. 193:783-784(2011).
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; FR687359; CBW74148.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5ANG6; -.
DR   STRING; 882378.RBRH_03119; -.
DR   KEGG; brh:RBRH_03119; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000007437; 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:CBW74148.1}.
FT   REGION          18..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        656
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1004 AA;  110507 MW;  44B5A6C3F0175BC0 CRC64;
     MPEPFNRQFG EWLVTTSGSA AAARRNAKTA ATASRTAPAR PTPTVGTPTA HATASPTRSR
     TREDKDRPLF EDIRFLGRLL GDVVREQEGD AVFDVVETIR QSAVKFRRED DIDAAKKLDK
     MLKALTPEQT VSVVRAFSYF SHLANIAEDR HHNRRRRIHA LAGSAPQAGT VAYALARLAK
     SGGESLSALK TFFDTGLIVP VLTAHPTEVQ RKSILDAQHD IARLLAEHDQ PLTARERAAN
     EALLRARVTS LWQTRMLRDS RLTVADEIEN ALSYYRTTFL DEIPALYADI EQALAEHGLP
     TRLPPFFQMG SWIGGDRDGN PNVTAATLER AITRQAAVLF QHYLEQVHRL GAELSVSELL
     AGSSDALKQL ADTSPDTSPH RVDEPYRRAL IGVYARLAAT ARALLGDAAV SIRGEHRDAA
     PYASPDAFRA DLQVLIDSLQ ARHGASLAAP RLSPLARAVE VFGFHLASID LRQSSDVHET
     VLTELFARAG VVDDYAALSE DDKLTLLLAE LAQPRALRLP YAEYSPLVHS ELAVLEATRV
     IRQRFGERAV RNYIISHTET VSDLVEVMLL QKETGLMHGS MPACGAAAGN GQHATHAGQG
     APRVSLMVIP LFETIADLRH APRIMQALLA LPGMDSIVRH QGGEQEVMLG YSDSNKDGGF
     LTSNWELYRA ELALVALFRE RGVRLRLFHG RGGTVGRGGG PTYQAILSQP PGTVDGQIRL
     TEQGEVIASK FGNPEIGRRN LETVVAATLE ATLQPHAQSP RALPQFEALM QTLSDAAMSA
     YRTLVYKTPG FTDYFFESTP IAEIAELNIG SRPASRKLHD PKHRRIEDLR AIPWGFSWGQ
     CRLLLTGWYG FGSAISAYLD AAPDALDREK RVALLRKMVK TWPFFSNLLS NMDMVLAKSD
     LAVASRYAQL VPDKKLRKQV FGQIVAEWHR TTDALAQITG HSSRLADNPL LARSIKNRFP
     YLDPLNHLQV ELLRRHRAGT TNARLRRGIH LTINGIAAGL RNTG
//