ID   A7IC33_XANP2            Unreviewed;       926 AA.
AC   A7IC33;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Xaut_0318 {ECO:0000313|EMBL:ABS65576.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS65576.1, ECO:0000313|Proteomes:UP000002417};
RN   [1] {ECO:0000313|EMBL:ABS65576.1, ECO:0000313|Proteomes:UP000002417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) 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; CP000781; ABS65576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7IC33; -.
DR   STRING; 78245.Xaut_0318; -.
DR   KEGG; xau:Xaut_0318; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; A7IC33; -.
DR   Proteomes; UP000002417; 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:ABS65576.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002417}.
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        588
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   926 AA;  103403 MW;  F43DE4CDA5CA1200 CRC64;
     MTSAVWSIEA PGDEEVKDRP LREDIRLLGR ILGDTVREQE GEEVFDLVER IRQTSIRFHR
     DDDETAREEL GALLEQLSSQ RAVDIIRAFS YFSHLANIAE DEHHIRRNRA HAIAGSAPRA
     GSLAYSLARA EALGIGPQQL TEFFSGAHMS PVLTAHPTEV RRKSTLNREM EIAALLDRRE
     RVVPTPAEQE QDEETLRRAV LTLWQTALLR RIKLTVLDEV ANGLSYYDYT FLSELPRLYC
     SIEDHVSQGG SEVALPSFLR IGSWIGGDRD GNPFVTADVL KETVRVHRDR ILAHYEQELT
     ELGAELSLGA RLIKVSPELA ELAARSPDRS QEHREEPYRL ALAYVLGRLR LTARHLKGEA
     PEGTEAEDAG SLAPYVNAAA LKADLDIIYA SLCDNGSKVL ARGRLRLLRR AVDCFGFHLA
     CIDLRQNSDV HERVVADLFE KVAPGTNYVG LDEEARIALL LQELATARPL ASPFLAYEDE
     TQSELAILRM AAEAHRALGR EVIPNCIISK AEGVSDLLEV ALLLKEVGLV TAEGTTALNI
     IPLFETIGDL QVCAKVMDRV LSLPAYRKLV SSRGDEQEVM LGYSDSNKDG GFVTSGWELY
     KAEIGLIEVF RAHNVRLRLF HGRGGSVGRG GGPSYDAILA QPGGAVNGQI RITEQGEIIA
     SKYSNPDMGR RNLEILVSAT LEASLLQPQF NAPRTEFLTA MEEISDTAFS AYRNLVYETE
     GFEDYFWSST VISEIATLNI GSRPASRAKT RSIEKLRAIP WVFSWAQCRL MLPAWYGFGS
     AVEAFAERRP DYGLSFLQAM YREWPFFRTQ LSNMDMVLSK SSLAIASRYA ELVPDVELRT
     QIFGRIRAEY ERTIKYVLAI MGQQKLLEDN PLLDRSIRNR FPYLDPLNHL QIELLRQHRA
     NSGDDKVLHG IQLSINGISA GLRNSG
//