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Database: UniProt/TrEMBL
Entry: A0A0S2FJK8_9GAMM
LinkDB: A0A0S2FJK8_9GAMM
Original site: A0A0S2FJK8_9GAMM 
ID   A0A0S2FJK8_9GAMM        Unreviewed;       920 AA.
AC   A0A0S2FJK8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-MAR-2018, entry version 14.
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=LC55x_0544 {ECO:0000313|EMBL:ALN83844.1};
OS   Lysobacter capsici.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=435897 {ECO:0000313|EMBL:ALN83844.1};
RN   [1] {ECO:0000313|EMBL:ALN83844.1, ECO:0000313|Proteomes:UP000059881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55 {ECO:0000313|EMBL:ALN83844.1,
RC   ECO:0000313|Proteomes:UP000059881};
RX   PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA   de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J.,
RA   Patel N., Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT   "Comparative genomics and metabolic profiling of the genus
RT   Lysobacter.";
RL   BMC Genomics 16:991-991(2015).
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}.
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DR   EMBL; CP011130; ALN83844.1; -; Genomic_DNA.
DR   RefSeq; WP_057920553.1; NZ_CP011130.1.
DR   EnsemblBacteria; ALN83844; ALN83844; LC55x_0544.
DR   KEGG; lcp:LC55x_0544; -.
DR   PATRIC; fig|435897.5.peg.534; -.
DR   KO; K01595; -.
DR   Proteomes; UP000059881; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 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:UP000059881};
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:ALN83844.1}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    581    581       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   920 AA;  100656 MW;  015F091107771C23 CRC64;
     MNVLLDTSDE PLRAVDFAST DALLRDDVKT LGALVGEILA EQRGPAFLDD VERLRRAAIR
     RREAQAPIGA LAEVLADIDL DQASDLVRAF ATYFQAVNLA ERVHRIRRRR DYERSGAGAQ
     PGGLRDAIGL LARQGVSAEE VAALLPRLRI EPVFTAHPTE AVRRALLEKE RTIVGCLVAD
     IDRNRTPTER RADRERIRLA LTASWQTAEA PAAKPSVADE FEHVGFYLSD VLYRVLPVYY
     ETFEDALREI YGERFGEGGA ALPDVLGFGT WVGGDMDGNP NVGADTIAAT LSGQRALVLN
     AYRNDLASLA ELLSQSVTRV RIDDAVLARV EDYRYQLPKA AALLKPRHAD MPYRNLLSLM
     AARLQATVEE SVHGYPDAPA FLADIALIER SLAANQGEHA GGFAVRRLRR RAECFGFHLA
     SLDLRQDSGT HDAALAALLD RPDWESLDVA TRATRLHSLL DGDAPPARAA ANAAQSTLEV
     FRAVARLRPR YGERAFGPYI VSMSRSAADA LAVLALAKTA GCVDGDGRVP LDVAPLFETV
     DDLDAAADTL RALFADPMYR AHLRARGNRQ VVMLGYSDSA KDGGMVASRW ALQQTQIALT
     ALAHDSQVRI AFFHGRGGSI SRGGGKTERA VIAAPRGSVD GYLRLTEQGE VIHRKYGIRA
     LALRNLEQTT GAVLRATLRP RAPEPREAGW RAIAAELAQR ARAHYRALVH EDPHFPAYFR
     AATPIDVIER LRIGSRPAKR AGVGDIGSLR AIPWVFAWSQ NRAGLTAWYG VGTGLERALA
     EHGRDALAEM ARDWPFFGTL IDDLEMVLAK SDPAIFERYS MLAADLPEGD LHARFHPGIA
     EEFERTRRAV LTIKGSEELL LGDHRLRQSI RLRNPYVDPI SLLQVDLLAR WRAAGRPDDG
     LQQALVATVN GIAAGVQNTG
//
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