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Database: UniProt/TrEMBL
Entry: A0A172YX30_9PSED
LinkDB: A0A172YX30_9PSED
Original site: A0A172YX30_9PSED 
ID   A0A172YX30_9PSED        Unreviewed;       881 AA.
AC   A0A172YX30;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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=A7J50_1285 {ECO:0000313|EMBL:ANF84720.1};
OS   Pseudomonas antarctica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=219572 {ECO:0000313|EMBL:ANF84720.1, ECO:0000313|Proteomes:UP000077829};
RN   [1] {ECO:0000313|EMBL:ANF84720.1, ECO:0000313|Proteomes:UP000077829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27494 {ECO:0000313|EMBL:ANF84720.1,
RC   ECO:0000313|Proteomes:UP000077829};
RA   Lee J.;
RT   "Complete genome sequence of Pseudomonas antarctica PAMC 27494.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; CP015600; ANF84720.1; -; Genomic_DNA.
DR   RefSeq; WP_064451041.1; NZ_CP015600.1.
DR   EnsemblBacteria; ANF84720; ANF84720; A7J50_1285.
DR   KEGG; panr:A7J50_1285; -.
DR   PATRIC; fig|219572.3.peg.1309; -.
DR   KO; K01595; -.
DR   Proteomes; UP000077829; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077829};
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:ANF84720.1}.
FT   COILED      169    189       {ECO:0000256|SAM:Coils}.
FT   COILED      765    785       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    143    143       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    548    548       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   881 AA;  98083 MW;  969A752DD4C28706 CRC64;
     MSDIDARLRE DVHLLGELLG NTIREQYGDD FLDKIEQIRK GAKADRRGSV SEQTAGEELS
     ASLNQLQESE LLPVARAFNQ FLNLANIAEQ YQLIHRRDES QPAPFESRVL PELLARLQSE
     GHSNESLARQ LARLEIELVL TAHPTEVARR TLIQKYDAIA AQLALQDHRD LTTAEREQIR
     ERLQRLIAEA WHTEEIRRVR PTPVDEAKWG FAVIEHSLWQ AIPNYLRKAD HALHAATGLH
     LPLEAAPIRF ASWMGGDRDG NPNVTAPVTR EVLLLARWMA ADLYLRDIDH LASELSMQQA
     SPALQAKVGD SVEPYRALLK QLRERLRATR QWAHTALTAN TPAPAEVLQN NRDLLDPLEL
     CYQSLHECGM GVIADGPLLD CLRRAVTFGL FLVRLDVRQD SSRHSAAMTE ITDYLGLGRY
     EDWDEEARIS FLTKELSNRR PLLPGYFKPS ADTAEVLNTC KEIAAAPAAS LGSYVISMAG
     AASDVLAVQL LLKESGVQRP MRVVPLFETL ADLDNAGPVM ECLLQLPGYR ARLHGPQEVM
     IGYSDSAKDA GTTAAAWAQY RAQERLVDIC REQQVELLLF HGRGGTVGRG GGPAHAAILS
     QPPGSVAGRF RTTEQGEMIR FKFGLPDIAE QNLNLYLAAV LEATLLPPPP PEPAWRHLMD
     ELAADGVSAY RAVVRENPQF VEYFRQSTPE QELGRLPLGS RPAKRRAGGI ESLRAIPWIF
     GWTQTRLMLP AWLGWEAALS KALERGEGEL LGQMREQWPF FRTRIDMLEM VLAKADADIA
     RLYDERLVQP DLLPLGAHLR DLLSQACSVV LGLTGQSQLL AHSPDTLEFI RLRNTYLDPL
     HLLQAELLAR SRQQEAAQDS PLEQALLVSV AGIAAGLRNT G
//
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