ID Q126H5_POLSJ Unreviewed; 970 AA.
AC Q126H5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
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 OrderedLocusNames=Bpro_3665 {ECO:0000313|EMBL:ABE45567.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE45567.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE45567.1; -; Genomic_DNA.
DR AlphaFoldDB; Q126H5; -.
DR STRING; 296591.Bpro_3665; -.
DR KEGG; pol:Bpro_3665; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR Proteomes; UP000001983; 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 Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 624
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 970 AA; 107864 MW; 7D128990C08C3D82 CRC64;
MLACEVQEQV QNQRVEMVIS ARARKVSENA KDGTPGKTGT RARDNERPLV EDIRLLGRIL
GDVIREQEGV TAYELIEQVR KLSVAFRRDA DQEADKALKK LLKGLSGEQT VSVIRAFTYF
SHLANLAEDR HHIRRRAVHE RAGDTQEGSI EVALARLRWA GISPKTIATT LAHSFVSPVL
TAHPTEVQRK SILDAERDIA QLLTARDDIK ALALATNAAK DALTPRELAA NEAQLRARVM
QLWQTRLLRF SKLTVADEIE NALSYYEATF LREIPKLYAN LERELGNQPV HSFLRMGQWI
GGDRDGNPNV SADTLNYALA RQAEVALRHY LTEVHYLGGE LSLSAMLVAV SPGMQALAES
SPDTNEHRKD EPYRRALTGV YARLAATLKE LTGGEAARHA VAPQNAYARA EDFLADLRTI
ETSLRSNHGE ALIAQRLHPL IRAVEVFGFH LATVDLRQSS DKHEEVVAEL LAVARIEPRY
PSLDEAAKRA LLIRLLNDAR PLRVISTIYS AHAQSELAIF EAARTARARF GKEAIRHYII
SHTETVSDLL EVLLLQKEVG LMHRTLDDKA TNDLIVVPLF ETIEDLRNAA PIMREYYALP
GIAQLVQRSG AEQDIMLGYS DSNKDGGIFT SNWELYRAEI ALVELFDQLA NSHNIQLRMF
HGRGGTVGRG GGPSYQAILA QPPGTVRGQI RLTEQGEVIG SKYANPEIGR RNLETLVAAT
LEATLLQPTK PATKAFLQAA AELSQASMAA YRALVYDTPG FNEYFFGATP IREIAELNIG
SRPASRKASQ KIEDLRAIPW GFSWGQCRLT LPGWYGFGAA IEKMLDAGGT PATRKEALAL
LQKMYKQWPF FRTLLSNMDM VLAKSDLALA SRYAELVADA RLRKKVFTAI EAEWHRTAEA
LTLITGEKQR LAGNAALQRS IRHRFPYIDP LHHLQVELVR RYREGKADQK VQTGIHISIN
GIAAGLRNTG
//
