ID   D1A204_THECD            Unreviewed;       892 AA.
AC   D1A204;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=Tcur_4129 {ECO:0000313|EMBL:ACY99657.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99657.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY99657.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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; Evidence={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; CP001738; ACY99657.1; -; Genomic_DNA.
DR   RefSeq; WP_012854440.1; NC_013510.1.
DR   AlphaFoldDB; D1A204; -.
DR   STRING; 471852.Tcur_4129; -.
DR   KEGG; tcu:Tcur_4129; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001918; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:ACY99657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918}.
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        552
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   892 AA;  98526 MW;  1B830F81F9ADB7AD CRC64;
     MRDSAAGQVP SEQRKALREE MPEPLRRDVR LLGAMLGEIL VEYGGPDLLE DVERLRHAVI
     DARQGRVSID EAAALVAGWD LERAELVARA FTVYFHLTNL AEEHHRIRAL RERDTDPAHP
     VSGSLAAAVA QIRGTGEHRL AQVLDGLEFR PVFTAHPTEA RRRAVVTAIM RISALLQDFN
     DPRKGAAERD EIRRQLREEI DLLWRTALRR HTQMDPLDEV RTAMAAFDET IFRVVPQLYR
     ALDSALDVGA SGPASGARPP RAHAYLRFGS WIGGDRDGNP YVTAQITREA VLIQSDHVLR
     ALENACTRIG RRLTVSSATT PPSAALRNAL DAARTAYPLL IAELAKRSPE EPHRQYLLYV
     AERIAATRAR HADMAYRSPE ELLADLRLVQ ESLAGAGAVR QAYGELQHLI WQTETFGFHL
     AELEIRQHSQ VHEKALAEVR AGGALSEMTE EVLDTLRVVS WIQRRFGVRA CHRYVVSFTR
     SADDIAAVYE LAESLGDHAP VLDVVPLFET GEDLDRAPSV LEGMLKLPAV QRRLAETGRR
     LEVMLGYSDS AKQLGPTSAT LRLYDAQAAL AAWAARNGIT LTLFHGRGGS LGRGGGPANR
     AILAQAPGSV NGRFKVTEQG EVIFARYGQR EIAKRHIEQV TNAIMLASTP AVEARAHEAA
     VRFRPLADRI SAAAQAAFRA LIETEGFAEW FARVSPLEEI SRLRIGSRPA RRTATRSLED
     LRAIPWVFAW TQTRVNLPGW YGLGSGLEAV LGGGDDEAGL AELQEAYRSW PLFAVMLDNA
     EMSLAKADRA IAERYLALGG RPELTERVLA EYDRTRSLVL AVTGHRRLLE NRRVLSRAVE
     LRNPYVDALS LLQLRALTAL REGVADDAER ARLEELLLLS VNGVAAGLQN TG
//