ID I4ESH5_9ACTN Unreviewed; 923 AA.
AC I4ESH5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:CCH86338.1};
GN OrderedLocusNames=MODMU_0888 {ECO:0000313|EMBL:CCH86338.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86338.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH86338.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH86338.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(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; FO203431; CCH86338.1; -; Genomic_DNA.
DR RefSeq; WP_014738946.1; NC_017955.1.
DR AlphaFoldDB; I4ESH5; -.
DR STRING; 477641.MODMU_0888; -.
DR KEGG; mmar:MODMU_0888; -.
DR PATRIC; fig|477641.3.peg.831; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000006461; 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:UP000006461}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 585
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 923 AA; 101309 MW; 0869328F9744547C CRC64;
MSEATVDVAD LHAPDDRESE NPLREDIRLL GRVLGEVIGE QAGADVLDLV EATRVEAFRI
RRSEVDRGEL AERLAGLEPR EANHVIRAFS HFSLLANIAE DVHHERRRRH HRREGSPAQP
GSLAASLQLL DAADLDPAVV ARELTGALVV PVVTAHPTEV RRKTVSQVQQ QISDLLQRRD
TDDPAWSAHL WREVLTLWQT ALLRLSRLRL ADEIDEALRY YDLSLFQVVP EINAELRQAL
QQRWPDAGLL ATPMLRPGSW IGGDRDGNPF VTADAVRRAT TSQAGTALRH HLAELVCLAD
ELSMSDRLVT PTEELYALAR AASDDSPFRA DEPYRQALRG IYRRLAATAL WVLGEVPGPA
PDAVLPAYEA PGELLADLET VDRSLRGHGA GALADDRLAR LREAVEVFGF HLCGLDMRQN
SSVHEEVLAE LLAWAGVCED YLALDEPARV ALLTGELQLR RPLVRPDAEL SELARGELDL
LRAAAEQVAL LGPDAIPNYV ISMCESVSDV LEVGVLLKEV GLLQLDAAGR PTSPLGISPL
FETIEDLQSA GATLAAMLDH PFYRALVAAR GDAQEVMLGY SDSNKDGGYL AANWALYRAE
LALVEVARAG GVRLRLFHGR GGTVGRGGGP SYEAIRAQPP GSVAGALRIT EQGEVIAAKY
ASPHLARRNL EALVAATLES TLLDIEGLGE DAEETYALFD DLAARARASY GALVHETPGF
VEWFRAATPI RELAELNIGS RPPSRKAGDK ITDLRAIPWV FSWSQARIML PGWYGTGTAL
ESWVGDSPDR LAQLQDLHAR WPFFRTVLSN MGMVLAKTDL ELAARYASLV PDAELRDRVF
SQITAEHERS VRMLLAITGD DHLLADNPSL ARSIRNRFPY LEPLHHLQVE MLRRRRGGDD
DELVRRCIQL SVNGVATALR NSG
//