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Database: UniProt/TrEMBL
Entry: A0A126NL81_9GAMM
LinkDB: A0A126NL81_9GAMM
Original site: A0A126NL81_9GAMM 
ID   A0A126NL81_9GAMM        Unreviewed;       903 AA.
AC   A0A126NL81;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AXG53_14190 {ECO:0000313|EMBL:AMJ57644.1};
OS   Stenotrophomonas sp. KCTC 12332.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1793721 {ECO:0000313|EMBL:AMJ57644.1};
RN   [1] {ECO:0000313|Proteomes:UP000066495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YM1 {ECO:0000313|Proteomes:UP000066495};
RA   Park H.;
RT   "Complete genome of Burkholderia sp.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014274; AMJ57644.1; -; Genomic_DNA.
DR   RefSeq; WP_062169230.1; NZ_CP014274.1.
DR   AlphaFoldDB; A0A126NL81; -.
DR   KEGG; stek:AXG53_14190; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000066495; 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:AMJ57644.1}.
FT   ACT_SITE        151
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        569
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   903 AA;  99902 MW;  B4D25FD3C621F889 CRC64;
     MNEYRSSVVF ATPDLPLRDD VRRLGALVGD LISEQVSPAF LDEVEDVRTA AIARRESQAP
     LAPLNTQLAG RSPRDAEALV RAFSTYFQVV NIAERVHRIR RRRDYQRAGT KRPQPDGLHD
     ALLALKAQGV TPEELAQWLP QIDIEPVFTA HPTEAVRRAL LEKEQLMVAA LVDNLDGQRT
     PGEQAADAAR FRMALTASWQ TADSSPVRPT VDDEREHVGF YLTRVLYRVI PVFYESLEQA
     LRDTWGRTLP LPRLLRFGTW VGGDMDGNPN VDAGTITATL NAQRSAVLGL YLKDMVALAS
     LLSQSTELVG VSDAVKARLQ EYQQLLPQVK SRPRHADMPY RLLNDRMRAR LQATLEDAPG
     AYASPEEFIH DIQLILDSLE ANKGKHAGWF SVRRLLWRVR TFGFHLARLD VRQESSVHSR
     ALAEVLGGQE AFDALDDAAR AQLLSPYAAG TEVLAQGEDE AGQRLDKVFA ALADARRRHG
     ADALGSYIIS MAHDRGDVLA VLALARRGGL VDADNAVPLD IAPLFETVDD LQRGTTTLHD
     LLADPVYRAH LAARNDVQMV MLGYSDSGKD GGIAASRWGL QHAQVELLDA AAEYGVKLTF
     FHGRGGSISR GGTKTTHAVN ASPRGSIGGR LRVTEQGEVI HRKYGIRALA LRSLEQSAGA
     VLRASLRPRA SEPREEQWKP VMALVAEQSS AAYRTFVGDA QFMNYFRKAT PIDVIERMTL
     GSRPSRRLGQ DAALTNLRAI PWVFAWSQAR AVIPGWFGVG SGLQAAADAG HEQTLREMAH
     DWPFFETFLD DMSMVLSKGD IHIAEQFSKL AGPLHEHFFP LIREELALTA HWVKRLSGQQ
     ELLEQDPRLA LSIRLRNPYI DPISILQVDL LQRWRASDRQ DEGLLRALVA CVNGVSQGVQ
     NTG
//
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