ID   F0MBG4_PSEPM            Unreviewed;       940 AA.
AC   F0MBG4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=Asphe3_06370 {ECO:0000313|EMBL:ADX71846.1};
OS   Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS   23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX71846.1, ECO:0000313|Proteomes:UP000008639};
RN   [1] {ECO:0000313|EMBL:ADX71846.1, ECO:0000313|Proteomes:UP000008639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC   {ECO:0000313|Proteomes:UP000008639};
RX   PubMed=21677849; DOI=10.4056/sigs.1393494;
RA   Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA   Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA   Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT   (Sphe3).";
RL   Stand. Genomic Sci. 4:123-130(2011).
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; Evidence={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; CP002379; ADX71846.1; -; Genomic_DNA.
DR   RefSeq; WP_013599788.1; NC_015145.1.
DR   AlphaFoldDB; F0MBG4; -.
DR   STRING; 930171.Asphe3_06370; -.
DR   KEGG; apn:Asphe3_06370; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008639; 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; 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.
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:ADX71846.1}.
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   940 AA;  103518 MW;  2C17C38FEFD5C87D CRC64;
     MAHTATNPET DLASELRADV RRVSTLLGES LVRQHGPELL DLVEQVRLLT KESKEAARGG
     ADATGPWSAH DVVAQVRELL GSLPIEQATD LVRAFAFYFH LANAAEQVHR VRGLRTRAEK
     DGWLAKTVAD IAGQAGPAVL QEVVNGLDVR PIFTAHPTEA SRRSVLDKIR KISDVLAQPT
     AEGTTGRRRQ DRQLAEIIDQ MWQTDELRQV RPTPVDEARN AIYYLGSILT DAMPEMLTEL
     SDLLGEHGVS LASQEAPIRF GSWIGGDRDG NPNVTAAVTR EILQIQNQHA VRISIGMIDE
     LISILSNSTA LAGADQELLD SIDADLKKLP GLDKRVLELN AQEPYRLKLT CIKAKLINTG
     KRVAADSNHE HGRDYNGTAE LLADLELVEL SLRNHSASLA ADGALARVRR AIASFGLHLA
     TLDIREHADH HHDAVGQLMD RLGGPGVRYA ELSREQRFEV LGSELASRRP LSGHPIKLDG
     AADGTYDVFR EIRRALRTYG PDVIETYIIS MTRGADDVLA AAVLAREAGL VNLFGEKPYA
     KIGFAPLLET VEELRASAEI VDQLLSDPSY RELVRLRGDV QEVMLGYSDS NKESGVMTSQ
     WEIHKTQRKL RDIAAKHGVR VRLFHGRGGS VGRGGGPTYD AILAQPNGVL EGEIKFTEQG
     EVISDKYSLP ELARENLELS LAAVLQGSAL HRDPRTSADQ RERYGHVMET ISDAAFNRYR
     HLIDDPDLPA YFLASTPVEQ LGSLNIGSRP SKRPDSGAGL GGLRAIPWVF GWTQSRQIVP
     GWFGVGSGLK AAREAGNSAQ LVEMWDNWHF FRSVLSNVEM TLAKTDMDIA GYYVSTLVPE
     ELHRIFRTIR EEYELTVAEV QNLTGENLLL DAQPTLKRSL EIRDQYLDPI SYLQVELLRR
     VRTEAAEKAE GISGAEIDER LQRAMLITVN GVAAGLRNTG
//