ID   G2IUI6_PSEUL            Unreviewed;       901 AA.
AC   G2IUI6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, 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   OrderedLocusNames=NH8B_0094 {ECO:0000313|EMBL:BAK74943.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK74943.1, ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT   Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012224; BAK74943.1; -; Genomic_DNA.
DR   RefSeq; WP_014085557.1; NC_016002.1.
DR   AlphaFoldDB; G2IUI6; -.
DR   STRING; 748280.NH8B_0094; -.
DR   KEGG; pse:NH8B_0094; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001274; 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:BAK74943.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001274}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   901 AA;  99183 MW;  D244AFFF20CD0FAE CRC64;
     MTDQDKDLPL RASIARLERL LGEVLLEQEG EQVYEEVRAI PADALTGGER SRSVLERLSP
     GATTALVRAC GLYSQLFNIA EDLHHTRRRR AHQIAGSAPQ QGSLAGALAR LKQDGVGFGQ
     LAATLADASV VAVLTAHPTE VQRQSVLDGH RAVRKFLSQL NSPELTPEEE SELEAKLKRV
     MLTLWQTSEI RPFKLSIRDE IENGVAYHPL TFFSAMPKLY ERLGRLIADH WEQQVELPSF
     LRVGSWIGGD RDGNPNVDAG VMRHAITRQA EEAFRHYFYE LAGLYRELSL SERHVSVSAA
     VQALSAASPD LAESRREEPY RRALATIEGR LSASAARLGV EARGRWTLGE PYADCAALVA
     DLQALVDSLR EHGSGLLAEG RLGRLLRSLD VFGFFLMPLD MRQHAAIHEA VVGELFARAG
     LEEYVALDEA ARVRVLLREL ATPRLLYSPY LTYSAEAEKE LAIFREAARI QREFGVDAIA
     QSIISNCATV SDILALALLL KEAGLIRLDN GIPQASINLV PLFETIADLQ NATLVMDALF
     ALPWYQQLLK SRGMIQEVML GYSDSNKDGG YLTSQWELYL AEQRLVQSFA AAGVKLKLFH
     GRGGSVGRGG GPSYEAIMAQ PAGSVAGRIR ITEQGEVIAS KYSDPDIGAR NLEALVAATL
     EASLSPHACH AVDEEVFNEL SGHAFTAYRE LVETPGFMQY FLEATPISAI AKLNIGSRPA
     SRKSLNSIRD LRAIPWVFSW AQSRVMLPGW YGFGSAVSAY LGRHGDEGLA RLQQAYASSP
     FFQVVLSNME QVMAKGDLNI AKGFADLVSD RRLADNLFGR ISEEWHKTQQ AFFAISGQQK
     LLEKNPTLGR SLDIRLPYLD ALNLLQTELL RRLREQPEDA EALYAIHLTI NGISAGLRNS
     G
//