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Database: UniProt/TrEMBL
Entry: A0A0M9VKC8_9MICO
LinkDB: A0A0M9VKC8_9MICO
Original site: A0A0M9VKC8_9MICO 
ID   A0A0M9VKC8_9MICO        Unreviewed;       890 AA.
AC   A0A0M9VKC8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-MAR-2018, entry version 16.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=XI38_12870 {ECO:0000313|EMBL:KOS09939.1};
OS   Microbacterium chocolatum.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS09939.1, ECO:0000313|Proteomes:UP000037737};
RN   [1] {ECO:0000313|EMBL:KOS09939.1, ECO:0000313|Proteomes:UP000037737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIT 101 {ECO:0000313|EMBL:KOS09939.1,
RC   ECO:0000313|Proteomes:UP000037737};
RA   Li X., Xu Y.;
RT   "Complete genome sequence of Microbacterium chocolatum SIT 101, a
RT   bacterium enantioselectively hydrolyzing mesomeric diesters.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOS09939.1}.
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DR   EMBL; LAVO01000014; KOS09939.1; -; Genomic_DNA.
DR   RefSeq; WP_053548723.1; NZ_KQ440293.1.
DR   EnsemblBacteria; KOS09939; KOS09939; XI38_12870.
DR   KEGG; mcw:A8L33_12580; -.
DR   PATRIC; fig|84292.3.peg.2613; -.
DR   KO; K01595; -.
DR   Proteomes; UP000037737; 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   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; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037737};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:KOS09939.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037737}.
FT   ACT_SITE    161    161       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    556    556       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   890 AA;  97263 MW;  3874BEF2CD7BA8A3 CRC64;
     MRELTNTEAI DLVGRFEAGQ ETPERMRADV RMLGSLLGKV LRESGSPGLF EDVERLRAAT
     IQAYTDETPE AFARAAAIAD SFSVARADEV ARAFTCYFHL VNLAEEHQRV RVLRERDGRP
     ERESASDSVA AAFVRLSAEV GDETALERLQ ALRFHPVFTA HPTEARRRAV SSSIRRLASL
     LDEHETSRRN GADERRAERR MLEEVDTLWR TAPLRPEKPS PTDEVRAVMA VFDETLYTAI
     PHVYRRVDDA LQGPGAGNRA PVVKPFVRIG SWVGGDRDGN PFVTASVTRK AAKIASEHVL
     IGLERTAERI GRGLTLDAAS TPPSEALLAL GRRLAAADEE AAGEIAQRSP NEPYRRILLL
     IARKLAATRA RDADLAYRDP EHLVADLRVI QDSLVQAGAA RQAYGHLQQL LWQVETYGFH
     LAELEVRQHS AVHARVLAEL EAGGERSELA DEVLDVFRSV AFLQERYGPR AAGRYIVSFT
     QSAEDLAAVH RLARFAVGPE GTPPVLDVIP LFETFADLQA APGILAEIVE HPEFASRLEA
     TGRRLEVMLG YSDSSKDVGP VAANLALYQA QAAISAWARE SGIELTLFHG RGGALGRGGG
     PANSAILAQP PHSVDGRFKL TEQGEVIFAR YGDPAIAMRH IDQVAAAILT ASAPSNEERN
     RAAADKYAEV AATMDVASRE RFFSLVKAPG FAPWFARVTP MEEIGLLALG SRPARRGLSV
     ESLADLRAIP WVFAWTQARI NLAGWFGLGS ALAAVGDEGL LQRAYAEWPL FRTMVDNVAM
     SLAKTDDRIA RQYLDLGDRD DLAELVRSEM ALTREWVIRV TGGTELLAGK PVLQRAVKMR
     SPYVDALSLL QLRALRALRA ADEGAPVDPE QQRLLLLSVS GVAAGLQNTG
//
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