ID   F6EYN8_SPHCR            Unreviewed;       898 AA.
AC   F6EYN8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   ORFNames=Sphch_2430 {ECO:0000313|EMBL:AEG50088.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG50088.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG50088.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG50088.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002798; AEG50088.1; -; Genomic_DNA.
DR   RefSeq; WP_013848328.1; NC_015593.1.
DR   AlphaFoldDB; F6EYN8; -.
DR   STRING; 690566.Sphch_2430; -.
DR   KEGG; sch:Sphch_2430; -.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   Proteomes; UP000007150; Chromosome 1.
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:AEG50088.1}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   898 AA;  97392 MW;  D1149E689253FF84 CRC64;
     MATPAPSSAP AITQNPDIRY LGRLLGDVIR AYGGEKIYKQ TEYIRSASVD RARGLHGADV
     VDTGLDALSL DDTLSFVRGF MLFSMLANLA EDRQGVAAEP GADVASAVEK LDSHGIGREA
     VLDLLSHALI VPVLTAHPTE VRRKSMIDHK NRIADLMLLK DGGRTETDEG ENLDEAIFRQ
     IALLWQTRPL RREKLFVADE IENVLAYFRD VFLPVLPALY ARWERVLGAR PQSFLRVGNW
     IGGDRDGNPF VQAPQLRLAL AKGCEAALTF YMGALHALGA ELSLSTELAH VPQSVLDLAD
     ASGDNSPSRQ DEPYRRAISG IYARLAATYQ ALIGKNPSRP STLKGQAYAI PADLRRDLVT
     VAQGLASEGG GALASGGALG RLIRAVETFG FHLATLDMRQ NSDVHQSVVA ELLKVAGVEA
     DYAALDEYAR IALLRRELAN NRPLGTRFSE YSEQTASELA IVHAAAEAHR VYGPQCITHY
     IISKAESVSD LLEVNIILKE AGLWRIGADG APQAAIMAVP LFETIADLEA APSIMTAYFG
     LPEIAGVVRG RGHQEVMIGY SDSNKDGGYI TSTWGLFQAS KALAPVFADA GTAMQLFHGR
     GGAVGRGGGS SFAAIQAQPK GTVQGRIRIT EQGEVIAAKF GTRDVAMTNL EAMTSATLLA
     SLEPEAISDR DAARFAAAMD QLSKTAFAAY RDLVYGTEGF KEFFRQLTPI QEISGLKIGS
     RPASRTKSTR IEDLRAIPWV FSWAQARVML PGWYGVGHAL SAFEDKVLLA DMAQHWSFLQ
     SALANLEMVL AKSDLGIAAH YLPLVEDQAR GAEIFDRIRD GWDKTHDGLL AATGQSRLLE
     KNPKLDSSIR LRLPYIEPLN LLQVELMKRH RSGEDDPRIK EGIELSINAI ATALRNSG
//