ID A0A0M3D4R6_9MICO Unreviewed; 897 AA.
AC A0A0M3D4R6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AAY78_18075 {ECO:0000313|EMBL:KKX96376.1};
OS Microbacterium sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1643443 {ECO:0000313|EMBL:KKX96376.1, ECO:0000313|Proteomes:UP000034223};
RN [1] {ECO:0000313|EMBL:KKX96376.1, ECO:0000313|Proteomes:UP000034223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKX96376.1,
RC ECO:0000313|Proteomes:UP000034223};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKX96376.1}.
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DR EMBL; LBCR01000034; KKX96376.1; -; Genomic_DNA.
DR RefSeq; WP_046749651.1; NZ_LBCR01000034.1.
DR AlphaFoldDB; A0A0M3D4R6; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000034223; Unassembled WGS sequence.
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; 2.
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:KKX96376.1}.
FT ACT_SITE 167
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 560
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 897 AA; 98330 MW; 4BA0DAFB0ECD078E CRC64;
MTPAHSFSEP TNTEAIRVIG RFEAGQGIPD AMRTDVRMLG QLLGQVLREA GGDDLFDDVE
RLRLATIQAY EDETSDAFER AAAIAESFTV ARADEVARAF TCYFHLVNLA EEHQRVRVLR
ERAGQPGRED TADTVATAYA RLRTEVGDDE ARRRLEGLRF HPVFTAHPTE ARRRAVSSSI
RRLSELLTQH DAASERGAEE HRARRRMLEE IDTLWRTAPL RSQKPTPTDE VRTVMGVFDE
TLFTTVPHVY RRIDDALRGD DSGASAPVVP AFVRIGSWVG GDRDGNPFVT ASVTREASQI
AADHVLRGLE RALGRIGRTL TLAADDTPPS AEVTALWERF AQTEPDLAAE LATRSPDEPH
RRVLLVLARR VADTRRGDGG QPYARPEELL ADLRAVQASL ADAGAKRHAF GGVQHLIWQV
ETYGFHLTEL EVRQHSQVHA KALAELDAGE AVSAQTEEVL DVFRAIADIQ HDRGLRAAGR
YVVSFTQAAS DLANVHRLAR YALGDDAPVL DVVPLFETFA DLQAAPGILA EAVTFPEFRE
RMAATGNRLE VMLGYSDSSK DVGPVAANLA LYEAQEKIAR WAQDNDIELT LFHGRGGALG
RGGGPANSAI LAQPPHSVDG RFKLTEQGEV IFARYGEPAI AMRHIDQVAA ATLLASSPTE
EERTSRAAER YAEVASAMDA ASRERFFSLV KAEGFASWFA TVTPMEEIGL LALGSRPARR
GLSVESLEDL RAIPWVFAWT QARINLAGWF GLGSALQAVG DEELLVEAYR EWPLLRTMID
NVAMSLAKTD ERIARQYLAL GDRDDLAQLV LDELALTRRW VIRLTGGTGL LENKPVLQRA
VQLRSPYVDA LSLLQLRALR ALRSADHGPT GSGADAEQQR LLLLSVSGVA AGLQNTG
//
