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
//