ID A0A1L3ZZY0_9SPHN Unreviewed; 893 AA.
AC A0A1L3ZZY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 03-MAY-2023, entry version 20.
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=BSL82_14500 {ECO:0000313|EMBL:API61183.1};
OS Tardibacter chloracetimidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Tardibacter.
OX NCBI_TaxID=1921510 {ECO:0000313|EMBL:API61183.1, ECO:0000313|Proteomes:UP000182063};
RN [1] {ECO:0000313|Proteomes:UP000182063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA Lee H., Ka J.-O.;
RT "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT A5.";
RL Submitted (NOV-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; CP018221; API61183.1; -; Genomic_DNA.
DR RefSeq; WP_072598814.1; NZ_CP018221.1.
DR AlphaFoldDB; A0A1L3ZZY0; -.
DR STRING; 1921510.BSL82_14500; -.
DR KEGG; sphj:BSL82_14500; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000182063; 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:API61183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182063}.
FT ACT_SITE 134
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 560
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 893 AA; 97264 MW; 3E988C9A8FFCFFA1 CRC64;
MVKARSQHLS QNEDVRYLGR LLGDVIRAYG GEELFRRTEY IRRASVDRHR GISGADAVDT
GLDRLSLDDT LSFVRGFMLF SMLANLAEDR HSRASQHWPS LASALDILDK QGVARAEVIR
LLDNGLIRPV LTAHPTEVRR KSLIDHRARI EALMTLRDNG ASTTPEGDDL EEAISRQIAL
LWQTRALRTD RLFVTDEVEN AVSFMRESFL PAMPRLYAAW DKLLEHRPKS FLTLGNWIGG
DRDGNPYVTA DALRLALRRQ AEAVLQFYLD QVHALGAELS IAVGLAPVDE ELLALAEASG
DTAPARLDEP YRRALSGIYA RLATTYERLT GHAPPRRSSL KGEAYAGPDA LRGDLTVIAH
SLGHSGEGLL ATGGALGRLI RAVETFGFHL ATLDLRQNAD VHERTVAALL AAAGVEQDYL
ALDEPGRVAL LRRELASPRP LTVPYADYDE ETAGELEIFR AAASAHALYG QGAITVAIIS
KAASVSDLLE LLVLLKEAGL YRPGPEPGAT IMPVPLFETI DDLEAAPQVM DEWLSIPEVA
ALAKARGYQE VMIGYSDSNK DGGYLTSNWS LALGSEALAR VFAEKGIALQ LFHGRGGAVG
RGGGSAFDAI RAQPAGTVNG RIRVTEQGEV IAAKYGDAEH AAANLEAMVA ATALASLAPP
VLAKKDDERF RAAMETLSAS ARNAYRALVY ETPHFPEFFR QATPIREISG LKIGSRPASR
TKSTRIEDLR AIPWVFSWAQ ARIMLPGWYG VGRALSSFDD KGLLREMAAG WPFFKTTLDN
MEMVLAKTDL AIARRYAGLV EDRALSESIF GTISEGWALT RDSLLDATGQ SRLLAHSPAL
DASIRLRLPY IEPLNLLQVD LIRRLRGGDS DEKVVTGIQL TINAIATALK NSG
//
