ID A0A0A1D0T9_9MICC Unreviewed; 939 AA.
AC A0A0A1D0T9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=ART_3224 {ECO:0000313|EMBL:AIY02823.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY02823.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY02823.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY02823.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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|HAMAP-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; CP007595; AIY02823.1; -; Genomic_DNA.
DR RefSeq; WP_038466167.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1D0T9; -.
DR STRING; 1494608.ART_3224; -.
DR KEGG; arm:ART_3224; -.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000030301; 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:AIY02823.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 597
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 939 AA; 103122 MW; 641D34585E5ACE72 CRC64;
MSSDLPTTAE NGAEDPQQDT DLRRDVRRVS TLLGESLVRQ HGPELLAMVE QVRLLTKESK
EAARGETGTG PWSANDVAEQ VREVLASLPL EQATDLVRAF AFYFHLANAA EQVHRVRSLR
SRPEKDGWLA KAVTEIADQA GTEALQKVVN ELDVRPIFTA HPTEASRRSV LDKIRKLSDI
LATPSEEGST ARARQDRKLA EIIDQMWQTD ELRKVSPTPM DEARNAIYYL RNILTDAMPE
VLTELSDLLG EHGVTLPPDA APLRFGSWIG GDRDGNPNVT SEVTREVLIL QNQNAVKISL
SLIDELLSVL SNSSALYGAD VALTDSIAAD LAKLPGFDPR VLELNADEPY RLKLTCIKAK
LINTQKRVAA DAYHEHGRDY SATSELISDL ELLESSLRNN SATLVADGAL ASVRRAISSF
GLHLATLDIR EHADHHHDAV GQLVDRVGEL GTPYAELDRA ERMAVLSTEL ASQRPLSGHP
IKLDGAANGT YDVFRVVRRA LRTYGPDVIE TYIISMTRGA DDVLAPAVLA REAGLVQLTG
ENRYAKIGFA PLLETVDELR ASAEIVDQLL SDPAYRELVR LRGNVQEIML GYSDSNKESG
VLTSQWEIHK TQRKLRDVAV KHGVNVRMFH GRGGSVGRGG GPTYDAIMAQ PNGVLEGAIK
FTEQGEVISD KYSLPELARE NLELSLAAVM QGSALHQAPR HSEDDLGRFG DLMEVMSDAA
FGTYRTLIDH DDLPAYFLAS TPVEQLGSLN IGSRPSKRPD SGAGLGGLRA IPWVFGWTQS
RQIVPGWFGV GSGLKAAREA GHGDELKEML EHWHFFSSTI SNVEMTLAKT DMAIAAHYVA
TLVPTELQHL FATIRAEYDL TVAEIQLLTG EAELLDNQPL LKRSLNVRDQ YLDPISYLQV
ELLRRVREAD ITKADVDERL QRAMLITING VAAGLRNTG
//
