ID K6Y623_9ALTE Unreviewed; 872 AA.
AC K6Y623;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ECO:0000313|EMBL:GAC19391.1};
GN ORFNames=GARC_2425 {ECO:0000313|EMBL:GAC19391.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC19391.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC19391.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC19391.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC19391.1}.
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DR EMBL; BAEO01000030; GAC19391.1; -; Genomic_DNA.
DR RefSeq; WP_007620161.1; NZ_BAEO01000030.1.
DR AlphaFoldDB; K6Y623; -.
DR STRING; 493475.GARC_2425; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000006327; 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; 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:GAC19391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006327}.
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 872 AA; 98159 MW; 16F089B66ECDA544 CRC64;
MSQVLDSQLT STVRNLGAVL GDTIRDQLGE QWLERIEAVR KDGRKAHQGD DHSAKRVKQL
FSELKNDELL TIGRAFSQFL NLANIAEQES NSSNDQDDPI DTLFSHLDAA DIQAETFEKA
LDHLNIELIL TAHPTEVTRR TLIHKHSELA KCLSKVHVSD ISGSERDKIE TRIAELISQA
WHTEEIRTIR PTPVDEARWG FSVIENSLWE AVPEFIRELD KRFVDKFDLP IPLDVSPVKF
GSWMGGDRDG NPFVTSKVTE QVLLLARKRA AKLFAKDIDI LQTELSMSDC DKNLREQVGD
ELEPYRAILR PLLEKLVKTQ EGIVEKLKDK PVDMSNWIDN KEQLLAPLMT CYHSLQACGM
SVIARGNLQD TIRRIHCFGV HLLKLDVRQD SERHADVFSE LTRYLGLGDY GQWSEEDKQA
FLLRELASKR PLFPPKWQPS DDVQEVLDTC KVIAQNGKDG FGIYIISMAS LPSDVLSVNL
LLKELGVTWP MPVAPLFETL DDLNAAASVT QKLFSIDWYR GYIQGHQHVM IGYSDSAKDA
GAMAAGWAQY ESQESLVALA EEHDIELTLF HGRGGTIGRG GLPAHAAILS QPPGSLTGGF
RVTEQGETIR YKFGMPILAQ RSLAMYASAI LEALILPPPA PKQEWRDAII KMAADGRDNY
RKIVRHDENF VPYFRVATPE QELGKLPLGS RPAKRKPTGG IESLRAIPWI FAWAQTRMVL
PSWLGSMKAV QTSLDAGKED TIKDMLANWP FFYSRLSMLD MVFSKADPKI SQEYDQNLVP
EELRHFGDAL RTELQESIDL LLQLLNQKTV MEGDPKGEMS MNIRASYLQP LHYLQIELLK
RTRALGDEHD PTLERAMMVT IAGIAVGMRN TG
//
