ID   D2QW47_PIRSD            Unreviewed;       942 AA.
AC   D2QW47;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=Psta_1244 {ECO:0000313|EMBL:ADB15922.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15922.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB15922.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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; CP001848; ADB15922.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2QW47; -.
DR   STRING; 530564.Psta_1244; -.
DR   KEGG; psl:Psta_1244; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   Proteomes; UP000001887; 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; 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; 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:ADB15922.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   942 AA;  106529 MW;  5AB648C45AA88D4E CRC64;
     MLKTRHDVCR PQAVYIHAKG GFEMAPVSNE LLRRDVRMLG DMLGEVMTEA AGPEALALVE
     EIRQLARRRR SGDHTAEPEL AEKIASLSMS DARIVARAFS IFFDLANLAE DRHRIRVLRS
     REQELHPVSL SESIGAAIGR LKESGFSAAE TQRAIDKMLI ELVFTAHPSE AKRRSIRAKL
     RRMRHALQEL DRTDLLPRER ARLESRIRTE LTVLWQTDFL RPSRPTVLEE VERGLSITPR
     LWEVVPQVYA SMRLALDTHY PGEGIRPGLF LRFGSWMGGD RDGNPNVTAP ITKQTLVWLR
     ERAISQHLAL TKTMYDFLSI SVREIDADST LNKGLEEASQ KWPGLAEALS ELAPLEVYRR
     WVTMIRWRLS QSSATTSCTS IPEGGYRDGE ELFADLKAMQ DSLRSHHSRL LADSELQRWL
     DLTTVFGLHL TRLDVRQDAR RYREVMTEIL SVAGIVENYA DLPEAERCAA LSRSIPWDHD
     LDREKLSPLA LETLDLFLVL RDAIAVFGPS CIGGHVISLT QCPSDVLNVL WLWRWAQSKA
     VRDSSVPTTD ELRIIPLFEK IDDLRNAPET MTSILEHPLY REHVTRVGDR QIIMVGYSDS
     TKDGGYLAAC WGLYQAQSGL QQVAHDHGVQ VTFFHGRGGS LGRGGGPAAR GILSLPPEAL
     DGTLRLTEQG EVLAERYDDT QVAFRHLEQV TWATLVASAL PGVQVKPSWL SMMETLSVQS
     FKAYRELVDQ PGFIAFFAAA TPIDEIENLP IGSRPSRRRG ERTLGDLRAI PWVFSWTQNR
     CMIPAWYGLG TALSEVKYKD RTAWQTICEM YRLWPFMQAT IDNAMLALAK ADMYIAQHYS
     ELAEDPAQRQ VCWELIARER DRTRQALLDL VGGSELLSKN PWFQGSIEVR NPYIDPLNLI
     QIELLRRRRS LTPEAPANEA EQLRDMLRLT VQGIAAGMRT TG
//