ID   I4BIU9_MYCCN            Unreviewed;       940 AA.
AC   I4BIU9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=Mycch_2433 {ECO:0000313|EMBL:AFM17206.1};
OS   Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM17206.1, ECO:0000313|Proteomes:UP000006057};
RN   [1] {ECO:0000313|EMBL:AFM17206.1, ECO:0000313|Proteomes:UP000006057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB4 {ECO:0000313|EMBL:AFM17206.1,
RC   ECO:0000313|Proteomes:UP000006057};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL   Submitted (JUN-2012) 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, ECO:0000256|HAMAP-
CC         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; CP003053; AFM17206.1; -; Genomic_DNA.
DR   RefSeq; WP_014815686.1; NC_018027.1.
DR   AlphaFoldDB; I4BIU9; -.
DR   STRING; 710421.Mycch_2433; -.
DR   KEGG; mcb:Mycch_2433; -.
DR   PATRIC; fig|710421.3.peg.2431; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006057; 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   Pyruvate {ECO:0000313|EMBL:AFM17206.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        599
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   940 AA;  103189 MW;  3C901AADC9C3CD36 CRC64;
     MAQTSDLAPI GSVQRTQGGR EATEPMREDI RLLGAILGDT VREQNGEETF DLVERARVES
     FRVRRSEIDR SELATLFDGI DVGEAIPVIR AFTHFALLAN VAEDIHRERR RAIHEAAGEP
     PQNSSLAATY LKLDGADLDA ATVADALTGA LVAPVITAHP TETRRRTVFD TQHRITELMR
     LRLHGHTTTD DGRDLERELR RHILTLWQTA LIRLSRLKIS DEIETGLRYY PAAFFDVIPE
     VNAQVRAALQ ARWPDAGLLE EPILRPGSWI GGDRDGNPNV TADVVRLATG SAAYTAFAHY
     LSELTALEQE LSMSVRLVHI TDALAALADA CHEPARADEP YRRALRVVHA RLTATARQIL
     DRRAEHELDL GMEAYEAPAE LLADLDVIDA SLRGHGSAVL ADDRLGRLRE AVRVFGFHLS
     GLDMRQNSDV HEEVVAELLA WAGVHTDYMS LSEPERVDLL AAELATRRPL TGPGAVGVPP
     ACGGLSELAR KELDIVSAAA RAVHVFGAQA VPNYIISMCR SVSDMLEAAI LLKEAGLLDA
     SSETPYAPVG IVPLFETIDD LQRGSATLEA ALDLPLYRAV VAARGDSQEV MLGYSDSNKD
     GGYLAANWAL YRAELDLVES ARKTGIRLRL FHGRGGTVGR GGGPSYEAIL AQPPGAVRGS
     LRITEQGEVI AAKYAEPRIA HRNLETLLAA TLEATLLDVE GLGDAAGPAY EVLDDLAERA
     QRAYAELVHE TPGFVDYFKA STPVSEIGAL NIGSRPTSRK PTTSISDLRA IPWVLAWSQS
     RVMLPGWYGT GTAFEHWIDD GNDPDARLEV LRDLYRRWPF FATVLSNMAQ VLAKSDLGLA
     ARYAELVDDE ALRRRVFDKI ADEHERTIRM YKMITGQDDL LADNPALARS VFNRFPYLEP
     LNHLQVELLR RYRSGDEDEL VQRGILLTMS GLATALRNSG
//