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Database: UniProt/TrEMBL
Entry: K6Z4H3_9ALTE
LinkDB: K6Z4H3_9ALTE
Original site: K6Z4H3_9ALTE 
ID   K6Z4H3_9ALTE            Unreviewed;       873 AA.
AC   K6Z4H3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=C427_4843 {ECO:0000313|EMBL:AGH46942.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH46942.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH46942.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH46942.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(2013).
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|ARBA:ARBA00001946,
CC         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; CP003837; AGH46942.1; -; Genomic_DNA.
DR   RefSeq; WP_007642619.1; NZ_BAES01000088.1.
DR   AlphaFoldDB; K6Z4H3; -.
DR   STRING; 1129794.C427_4843; -.
DR   KEGG; gps:C427_4843; -.
DR   PATRIC; fig|1129794.4.peg.4825; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011864; 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; IPR033129; PEPCASE_His_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.
DR   PROSITE; PS00393; PEPCASE_2; 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:AGH46942.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        538
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   873 AA;  98145 MW;  ED2ED0DAC76544D3 CRC64;
     MTQALDSQLV GTVRNLGAVL GDTIRDQLGE QWLERIEAVR KDGRKAHQGD EESAKRVKQL
     FTELKNDELL TVGRAFSQFL NLANIAEQEF NSNNDQVDPM DTLFSHLDQA DIKADTFEKA
     LQHLNIELVL TAHPTEVTRR TLIHKHSELA KCLSKVHVSD INEVERDKIE TRIAELISQA
     WHTEEIRTIR PTPVDEARWG FSVIENSLWE AVPDFIRELD KRFVDKFGLS IPLDVSPVKF
     GSWMGGDRDG NPFVTSKVTE QVLLLARKRA AKLFAKDIDI LQTELSMSDC DDDLRAKVGD
     ELEPYRAILR PLLEKLVKTQ TGIVEKLKGI PVDMTDWVDN KEQLLVPLMT CYHSLQACGM
     SVIAQGHLQN TIRRIHCFGV HLLKLDVRQD SERHADVFSE LTRYLGLGDY GQWSEDDKQA
     FLLKELGSKR PLFPPAWQPS EDVQEVLDTC KVIAQNGKDG FGIYIISMAS LPSDVLSVNL
     LLKELGVTWP MPVAPLFETL DDLNAAASVT KKLFSIDWYR GYIQAHQYVM IGYSDSAKDA
     GAMAAGWAQY ESQEALVALA EENDIELTLF HGRGGTIGRG GLPAHAAILS QPPGSLTGGF
     RVTEQGETIR YKFGMPILAQ RSLALYASAI LEALILPPPA PKQAWREAMI KMAADGRDNY
     RQIVRHDENF VPYFRVATPE QELGKLPLGS RPAKRKPTGG IESLRAIPWI FAWAQTRMVL
     PSWLGVMKSV QSSLDAGKED TIQDMLANWP FFYSRLSMLD MVFAKADPKI SQEYDKSLVP
     KELRHFGDAL RTELQQSIDL LLKLLDQKTV MESDPKGSVS MNIRASYLQP LHYLQIELLK
     RIRQLDDKEH DATLERAMMV TIAGIAVGMR NTG
//
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