ID   D7A3G7_STAND            Unreviewed;       928 AA.
AC   D7A3G7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Snov_2431 {ECO:0000313|EMBL:ADH89726.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS   12100 / NBRC 12443 / NCIMB 10456).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Ancylobacter.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89726.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|EMBL:ADH89726.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC   12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA   Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA   Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA   Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic and
RT   methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT   8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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; CP002026; ADH89726.1; -; Genomic_DNA.
DR   RefSeq; WP_013167230.1; NC_014217.1.
DR   AlphaFoldDB; D7A3G7; -.
DR   STRING; 639283.Snov_2431; -.
DR   KEGG; sno:Snov_2431; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006633; 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:ADH89726.1}.
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   928 AA;  102706 MW;  C0FB2E8731CA3084 CRC64;
     MSVALTIALP DAELDADGEL DLSLRDDIRM LGRVLGDTLR DQEGEPTFEL VERIRRVSTR
     FHREEDEGAR HELEAILNQL DPEQTVTIVR AFSYFSHLAN IAEDQNVIRR MRAAAAAGNG
     GPPSVARAIE KARAHGVSSA ELRGFFDTAL ASPVLTAHPT EVRRRSTLTH EMCIAELLAD
     RARLDPTPEE QELADDELRR RVLMLWQTNL LRRTKLTVLD EVANGLAYYD YTFLRQLPKL
     YAAVEDRLAA LDGSGEASEL ASFLRIGSWI GGDRDGNPFV TADVTRETLR MQSAQAVRFY
     LEELDALGGE LSISTIRVKV SGELMGLVDA SSDGSPHRRN EPYRLATGVI TTRLRATAFR
     LEIADLLGIT EKPAAAPYAS AQELRADLDI IDRSLRTHGS SAIARGKLRA LRRAVDCFGF
     HLAVLDSRQN SDVHERCVAE LFEVAAPGTD YKGLPEGTRV ALLLRELATA RPLTSPFVAY
     SDETVGEMAM LRTCARIHQI YGPEAIQTCI ISKAEGVSDM LELALLLKEV GLVDPAGTAA
     VNIVPLFETI EDLRNAARVM EQMFRLPEYR KLVDSRGGVQ EVMLGYSDSN KDGGFVTSGW
     ELYKAEIELI EVFKRHGVRL RLFHGRGGSV GRGGGPSYDA ILAQPGGAVQ GQIRITEQGE
     IISSKYSNPA VGRGNLEILA AATMEATLLS GDAKAPREEY LSVMEKISDA AFKAYRALVY
     ETPRFEDYFW ESTVINEIAT LNIGSRPASR KKTRRVEDLR AIPWVFSWAQ CRLMLPGWYG
     FGTAVGEWLK ANPDGLPLLQ EMYREWPFFR TQLSNMDMVL SKSSIAIASR YAELVEDVEL
     RESIFGRIRA EHQAAIDALL SIAQQPKLLG SNPLLDRSIR ARFPYIDPLN HVQVGLLRAY
     RGNDTDEKVL QGIQLTINGI SAGLRNSG
//