ID   CAPP_PSET1              Reviewed;         881 AA.
AC   Q3IBX6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=PSHAb0314;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CR954247; CAI89354.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3IBX6; -.
DR   SMR; Q3IBX6; -.
DR   STRING; 326442.PSHAb0314; -.
DR   KEGG; pha:PSHAb0314; -.
DR   PATRIC; fig|326442.8.peg.3222; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   BioCyc; PHAL326442:PSHA_RS16355-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome II.
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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..881
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000129837"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   881 AA;  98998 MW;  CB477510EE6D3F80 CRC64;
     MSEQYAALRG NVNLLGQLLG QTIKDAQGQA ILDKVEEIRA LSKSSRSGNE NDRKTLIKVL
     HALSDEELLP VARSFNHFLN LANVAEQFHT VSRFNDVGFC QLNPLTQTLK TLATKANNGQ
     LNHNHLADTL SKLHINLVLT AHPTEVTRRT IINKHVELSD CLASLERTDN LAQEREAILN
     RIAQLISQAW HTDDIRRSRP TPVDEAKWGY AVIENSLWHA VPRFLREFSQ HVKEHLSLEL
     PINYSPIEFT SWMGGDRDGN PYVTAQVTKE VLDHGRWMAL DLYGRDLETL STELSMSDAS
     DELIALAGQE FEPYRCVIKT LKNQVLETVM HLGAKIKNQR SEAQDLITDI NQIKHPIEVC
     YRSLLKCNMK VVADGLLLDV LHRLNSFGLR LAKLDVRQDS SRHGDVFSEL TRYLGLGDYN
     QWQEQDKQAF LLTELNSRRP LIPKRWQPSP EVQEVLDTFD VIAQQDEQTF GLYIISMART
     ASDILAVQLL LKESGCSFKL PVAPLFETLD DLNDGHNVIT TLLDNDWYRG QINNTQNVMI
     GYSDSAKDAG MMAAGWAQYE AMDKLVQLAD KRGIELVLFH GRGGTVGRGG APAAQALHSQ
     PPGSLKGGLR VTEQGEMIRF KFGLPDVALQ SLNIYAGAVL QSNLLPPPEP KPQWREVMAL
     ISEESCEHYR NVVRHDENFV PYFRMATPEL ELSKLPLGSR PAKRNPTGGV ESLRAIPWIF
     AWSQNRLMLP AWLGALTGLQ AALAKYGVET LQEMSLQWPF FRSRLEMLEM VFSKADSWLS
     EHYDNALVED MYKPLGVTLR KELAEAISLV QSLSPQKSLL ADQPWIKESI ALRNPYTDPL
     NVLQVELLRR ARSSDNGSEG DIDNALMITM TGIAAGMRNT G
//