ID K0MA42_BORPB Unreviewed; 982 AA.
AC K0MA42;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:CCJ47748.1};
GN OrderedLocusNames=BN117_0415 {ECO:0000313|EMBL:CCJ47748.1};
OS Bordetella parapertussis (strain Bpp5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ47748.1, ECO:0000313|Proteomes:UP000008035};
RN [1] {ECO:0000313|EMBL:CCJ47748.1, ECO:0000313|Proteomes:UP000008035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ47748.1,
RC ECO:0000313|Proteomes:UP000008035};
RX PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT "Comparative genomics of the classical Bordetella subspecies: the evolution
RT and exchange of virulence-associated diversity amongst closely related
RT pathogens.";
RL BMC Genomics 13:545-545(2012).
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; HE965803; CCJ47748.1; -; Genomic_DNA.
DR RefSeq; WP_015038805.1; NC_018828.1.
DR RefSeq; YP_006894480.1; NC_018828.1.
DR AlphaFoldDB; K0MA42; -.
DR KEGG; bpar:BN117_0415; -.
DR HOGENOM; CLU_006557_2_0_4; -.
DR Proteomes; UP000008035; 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}.
FT ACT_SITE 182
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 627
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 982 AA; 107941 MW; 4CC69FF3516F807D CRC64;
MAAYNAPVSN CQFRLTHILP IPQRQGAPTD PFQMNAIRQQ SDSAEPLRHD IRLLGRCLGE
VIQACEGKRV YDTIETLRRT AVRFRRAGDP ADDKLLQARV KQLRGNDPNS VARAFSYFLH
LSNIAEDRDQ NRRQRDRALA GAGPERGSLR QAIESLKAQG VNNARIRRLL SEACVMPVLT
AHPTEVQRKS TLDVHREISS LLVQRERELT ADELSELDLA LIGQVATLWQ TRMLRYTRLT
VADEIENALS YYRSTFLNVI PRVYGDLARL LNREPVKPFT PPPPPLEPFL RMGSWIGGDR
DGNPNVDAAT LERALLRQAT VLFEHYLQEV HALGAELSAS TLLIEADPAL LALADAGGDD
SPHRRDEPYR RALIGIYARL AATARHLTGQ ELARRATVPA APYDTPDALA ADLAVIAASL
SAHHGAPIAR LRLSGLQQAV TVFGFHLATV DLRQSSDVHE RVLAELFARA GDGIDGQAVD
YLALDEAARV AVLRRELAHA RPLASPWIAY SEETASELAV LRAAAAGRAR YGIQAVLQSI
VSHTETLSDL LEVLVLQKEA GLIAPPGETI APGDGLMVVP LFETIPDLQR GPEIMAAWLD
LPEVRQRVRL AQGDTQEVML GYSDSNKDGG FLTSNWSLYQ AERALVDVFS ARSVRLRMFH
GRGGSVGRGG GSSYDAILAQ PPGTVAGQLR LTEQGEVIQS KYKDAEVGRW HLELLVAATL
ESSLAPQAAA TSAEDAHMQQ HAPAMSFMSE LAQRTYRGLV YDTPGFADYF FAATPISEIA
GLNIGSRPAS RKKGQHIEDL RAIPWGFSWA QCRLMLTGWY GMGAAIEAYL ETGAQGAPRS
RRARLAQLRE MASDWPAFRT LLSNMEMVLA KSDLAIAAGY AQLVPRRGLR ERVFGAITAE
HGRTLAMLRL LTRRELLADN PGLMASLRER FAYIDPLNYL QIELIKRHRA AQRRAGDDAD
IRVPRAIHLT INGIAAGLRN SG
//
