ID A0A132PRQ4_9MYCO Unreviewed; 931 AA.
AC A0A132PRQ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AFM11_06200 {ECO:0000313|EMBL:KWX25019.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX25019.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX25019.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX25019.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-2015) 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:KWX25019.1}.
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DR EMBL; LGTW01000003; KWX25019.1; -; Genomic_DNA.
DR RefSeq; WP_067845232.1; NZ_LGTW01000003.1.
DR AlphaFoldDB; A0A132PRQ4; -.
DR STRING; 59750.AWC31_29475; -.
DR PATRIC; fig|59750.3.peg.4432; -.
DR Proteomes; UP000070612; 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:KWX25019.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070612}.
FT REGION 1..23
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 593
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 931 AA; 102702 MW; 9BBC878E63D0EFB3 CRC64;
MVDGPDTTLE PIGSVHRTPV GRDATEPMRE DIRLLGAILG DTVREQNGEA VFDLVERARV
ESFRVRRSEI DRAELAGLFG GIDIHRAIPV IRAFTHFALL ANVAEDIHRE RRRAVHVAAG
EPPQDSSLAA TYLKLDSADL DAHAVADALT GALVSPVITA HPTETRRRTI FDTQHRITEL
MRLRLHGHTH TEDGRDIEIE LRRHILTLWQ TALVRLSRLK ISDEIETGLR YYPAAFFQVI
PQVNAEVRDA LQARWPGTEL LTEPILRPGS WIGGDRDGNP NVTADVVRLA TGRAAYTALA
HYFTEITALE EELSMSARLV KVTDGLTALA DACHEPARAD EPYRRALRVI HARLTATAQQ
ILDEQPEHQL DLGLAPYPTP VEFLADLDTV DASLRANGSA VVADDRLARL REAVRVFGFH
LSGLDMRQNS EVHEQVIAEL LSWSGVHADY ASLPEADRVE LLAAEISTRR PLIGEDADLS
ELARKELSIV GAAARAVKVL GPQAVPNYII SMCQSVSDML EAAVLLKEAG LLNLTGPQPY
CPVGIVPLFE TIDDLQRGSS ILEAALDLPV YRTMVACRGR HQEVMLGYSD SNKDGGYLAA
NWALYRAELD LVESARKTGI RLRLFHGRGG TVGRGGGPSY DAILAQPPGA VNGSLRITEQ
GEVIAAKYAE PRIAHRNLET LLAATLESTL LDVEGLGEEA EPAYRVLDEL AARAQRAYAE
LVHETPGFVD YFKASTPVSE IGALNIGSRP TSRKPTTSIA DLRAIPWVLA WSQSRVMLPG
WYGTGTAFEE WVAEDDSRLA VLQDLYERWP FFRTVLSNMA QVLAKADMGL AARYSELVDD
DDLRARVFDK IVAEHDRTIR MHRLITGQDD LLADNPALAR SVFNRFPYLE PLNHLQVELL
RRYRSGDTDE LVQRGILLTM SGLATALRNS G
//
