ID A0A260C217_9NOCA Unreviewed; 943 AA.
AC A0A260C217;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CH275_00355 {ECO:0000313|EMBL:OZD10190.1};
OS Rhodococcus sp. 06-235-1A.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2022508 {ECO:0000313|EMBL:OZD10190.1, ECO:0000313|Proteomes:UP000215839};
RN [1] {ECO:0000313|EMBL:OZD10190.1, ECO:0000313|Proteomes:UP000215839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06-235-1A {ECO:0000313|EMBL:OZD10190.1,
RC ECO:0000313|Proteomes:UP000215839};
RA Savory E.A., Fuller S.L., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZD10190.1}.
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DR EMBL; NOYI01000002; OZD10190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260C217; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000215839; Unassembled WGS sequence.
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:OZD10190.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 605
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 943 AA; 103787 MW; C2675AB9167E63D1 CRC64;
MSESSYESVG SPAFVPPTAQ GRELTEPLRE DIRYLGGILG EIIREHEGND VFDLIESARV
ESFAVRRSEI ERDDSVGRYT DVEVAQAVPL IRAFSHFSLL ANLAEDLHRE RRRAIHLDRE
DPPQDSSLDA TWLKIDAAAP SREQVAAALT DALVAPVITA HPTETRRRTI FDVQSKITEL
MRRRDIATAA REGKAASAAK ELAAIDVQIR RQVLTLWETA LIRLSRLRIQ DEIEVGLRYF
ESSLFDVMPA LNADVRAALR ARWPEDDLLP RPILRPGSWI GGDRDGNPNV TAEVVHTATH
QAGYVAFEHY LDELVALEKE LSMSARLVDV TEDLAALAGA SAEPDDRRSD EPYRVAVVGI
RARLTATAEA VLDAVPVSGV DLGASKYDGP QDILDDLDII DRALRADGDA LIADDRLLRL
RRSVETFGFH LQALDMRQNS ETHEEVVAEL LAWAGVHPDY LSLGEDERVS VLSQELATRR
PLVGPNAHLS ELATKELGIV KAAKEAIDHL GPDTIQNYII SMCQSVSDML EAALLLKEAG
IFDPGTDGSS PTSTVGVVPL FETIEDLQQG AATLLATLDV PIYRALVAGR GMNQEVMLGY
SDSNKDGGYL AANWALYRAE LDLLEASRKT GIRLRLFHGR GGTVGRGGGP SYDAILAQPP
GVVQGSLRLT EQGEIIAAKY AEPSLARRNL ESLVAGTLES TLLDVEGLGD GAEAAYDILD
DLAAKARAAY GRLVHEEPGF VEYFRTSTPV AEVGELNIGS RPASRKPTNS VYDLRAIPWV
MSWSQCRVML PGWYGTGSAF EEWVGDDDSK LDVLTDLYRK WPFFQTVLSN LAQVMAKSDL
GIAARYAELV PDADLRARIF GMIEAEHATT VRMYLKITGH SRLLEDNPSL ERSVHNRFPY
LEPLNQMQVE MLRRYRNGDD DERVKRGILL TMNGLATALR NSG
//
