ID   I0HVF0_RUBGI            Unreviewed;       943 AA.
AC   I0HVF0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:BAL96987.1};
GN   OrderedLocusNames=RGE_36480 {ECO:0000313|EMBL:BAL96987.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL96987.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL96987.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL96987.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0HVF0; -.
DR   STRING; 983917.RGE_36480; -.
DR   KEGG; rge:RGE_36480; -.
DR   PATRIC; fig|983917.3.peg.3564; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000007883; 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:BAL96987.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   943 AA;  105474 MW;  F6CC8A9C65D37E47 CRC64;
     MPRRPSTAAA PRKTSPHQSA ADAAEKNRPL VEDIRLLGRI LGDVIREQEG TEAYELIERV
     RQLSVAYRLK ADASAGRVLD RLLKNLSADQ TVSVIRAFSY FSHLANIAED RHHVRRRRVH
     EREGHLQEGS LAMAIDRLHA ADHHNADIAR MLDGAYLSPV LTAHPTEVQR KSILDAERAV
     AELIGQRDEQ LTEDQRRENE ELLRARVTQL WQTRMLRTAK LTVADEIENA LGYYPSTFLR
     EIPRLYRELE RALPGHPVAP FLRMGHWIGG DRDGNPNVDA STMRRALARQ GETALRFYLD
     EVHALGVELS TSAMLAPVTP AMQALAERSP DRSVHREDEP YRRALIGLYA RLAATLQALT
     GAAAPRTAVA PQPPYADAAE FLADLRIIEA SLRHHHAQAL IAPRLAPLMR AVQVFGFHLA
     TLDLRQSSDK HEAVVAELLR VARLEPDYAA LDEPARRALL LRLLDDARPL RVRGAEYSAL
     ATSELEVFET AREGRERYGR EALRHYIISH TEDVSDLFEV LLLQKEAGLL RGTLDRDATA
     DLIVVPLFET IGDLRQAAAI MRAYYALPGI TAMVVRSGAE QDVMLGYSDS NKDGGFFTSN
     WELYRTEVAL GEFFATLHRE HGIRMRLFHG RGGTVGRGGG PSYQAILAQP PGTVNGQIRL
     TEQGEVIGSK YANPEIGRRN LETLVAATLE ATLLHPTKSA PKTFLDAAAR LSDASFAAYR
     ALVYETPGFV DWFFAATPIR EIAELNIGSR PASRKATRAI EDLRAIPWSF SWGQCRLALP
     GWYGFGSAVE AFLGDETTQP ARLELLQRMY RQWPFFRTLL SNLDMVLAKT DLRIAARYVE
     LVEDKRAAKR VFTTIRAEWE RVGRALEQIT GEASRLQSNP TLARSIEHRF PYLDPLNHLQ
     VELMRRFRQR KPDAAADDPA VARLQRGIHI SINGVAAGLR NTG
//