ID   B1KND1_SHEWM            Unreviewed;       878 AA.
AC   B1KND1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=Swoo_0327 {ECO:0000313|EMBL:ACA84628.1};
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA84628.1, ECO:0000313|Proteomes:UP000002168};
RN   [1] {ECO:0000313|EMBL:ACA84628.1, ECO:0000313|Proteomes:UP000002168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) 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; CP000961; ACA84628.1; -; Genomic_DNA.
DR   RefSeq; WP_012322977.1; NC_010506.1.
DR   AlphaFoldDB; B1KND1; -.
DR   STRING; 392500.Swoo_0327; -.
DR   KEGG; swd:Swoo_0327; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000002168; 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:ACA84628.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002168}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   878 AA;  98843 MW;  E65F827C57BC9501 CRC64;
     MTDMYASLRS NVGTLGQILG ETIRTNLDDP FLDKIEQIRQ LAKSSRQGDE ASREEMLKLL
     AALPDDELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVEQLLG RVLSSNIEQD
     KMLDCLQNLD IDLVLTAHPT EISRRTLIQK YASVVDSLAA LENPLLTERE KKQQHLRLRQ
     LIAQIWHTNE IRHERPTPVD EARWGLSTIE VSLWQAIPDF LRQLNEQVEE RTGKQLPIDI
     APVRFSSWMG GDRDGNPFVT AQVTQEVLDR NRHTAARLYL KDVVLLVNDL SMEEANDELL
     ALTNNSHEPY RDVLRGIRQK LRNTIDYLNE RLEGHQPEVD KNSIIWNEDD LKAPLMMLYK
     SLSDSGMSLI ANGLLLDMLR RIACFGIHML RLDIRQDAQR HCDVVAELTR YLGMGDFNHW
     DENEKQAFLL RELSSKRPLI PSNWQPSEDV AEVVSTCRLI ATQPARALGS YVISMASKPS
     DVLTVLLLLK ETGCPHPMRV VPLFETLDDL NNASSCMSAL FAIDWYRGYT KGHQEVMIGY
     SDSAKDAGVM AAAWAQYHAQ EQLVEVSRQA DVKLTLFHGR GGTIGRGGGP AHEAILSQPP
     GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPAPKP EWRACMQRLA
     EESVAAYRSI VREEPDFVAY FRAATPEVEL GKLPLGSRPA KRRVDGGIES LRAIPWIFAW
     SQNRLMLPAW LGAGEALQAA SDRGEMELLQ EMEQKWPFFK TRISMLEMVY AKAEPNLAKY
     YETCLVPENL HHLGDALRGR LATGVKAVLA LTQSQALMEH TPWNRESVTL RNPYIDPLNF
     MQAELLARTR KDEVQSTNVE LALMLTIAGV AAGMRNTG
//