ID   K9YWA8_DACS8            Unreviewed;      1007 AA.
AC   K9YWA8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-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   ORFNames=Dacsa_1744 {ECO:0000313|EMBL:AFZ50408.1};
OS   Dactylococcopsis salina (strain PCC 8305) (Myxobactron salinum).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Dactylococcopsis.
OX   NCBI_TaxID=13035 {ECO:0000313|EMBL:AFZ50408.1, ECO:0000313|Proteomes:UP000010482};
RN   [1] {ECO:0000313|EMBL:AFZ50408.1, ECO:0000313|Proteomes:UP000010482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8305 {ECO:0000313|EMBL:AFZ50408.1,
RC   ECO:0000313|Proteomes:UP000010482};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Daligault H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Dactylococcopsis salina PCC 8305.";
RL   Submitted (APR-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; CP003944; AFZ50408.1; -; Genomic_DNA.
DR   RefSeq; WP_015229405.1; NC_019780.1.
DR   AlphaFoldDB; K9YWA8; -.
DR   STRING; 13035.Dacsa_1744; -.
DR   KEGG; dsl:Dacsa_1744; -.
DR   PATRIC; fig|13035.3.peg.1974; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010482; 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:AFZ50408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010482}.
FT   ACT_SITE        189
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        650
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1007 AA;  116022 MW;  E079CDD01D0AE38D CRC64;
     MSSLLQASSE DTNDASRDQF LDRRIKLIEK LWESVLRAEC GQELVNLLQQ LRSMGSPEGQ
     ATGLPTSSVP QLIEELPLND AVRAARAFAL YFQLINIVEQ HYEQREQQLN RLGDEEKNNK
     QFSHQKEAEP QHSLLGAELL EKTWQGNSTY QKAGTFNWLF PYLKRLNVPP QQVQRLLNQL
     EVRLVFTAHP TEIVRQTIRK KQRRIAKILE QIDYNEATTK SLNFFESPEA VESTEQLEEE
     IRLWWRTDEL HQFKPEVLDE VDYALHYFQE VLFDTMPQLA KRLKKALKGS FKELTPPRNH
     FCRFGSWVGA DRDGNPSVTP EVTWETACYQ RGIVLERYLH SVKQLTTLLS LSLHWSDVLP
     ELLESLEDDR AVMPEVYERL AIRYRREPYR LKLAYIEKRL EHTIQRNQSL YSGEQSQQEA
     IKKHPKTIYK SDADFLAELK LIQRNLIETG LACQDLEDLI AQVEIYGFNL AELDMRQESS
     RHSETLDEIT EYLQILPQSY HQLSESERVK WLSEELQTRR PLIPGELPFS EKTQETVETF
     RLLKKLQQEF GTQVCRTYII SMSHEVSDIL EVLLLAKEAG IYDPATGSCS LQVVPLFETV
     DDLLSAPEIM KALFELPLYR ACLAGGYGLE KASNQYDIQE VMLGYSDSNK DSGFLSSNWE
     IHKAQKALQS LAEGYGVSLR IFHGRGGSVG RGGGPTYEAI LAQPSSTING RIKITEQGEV
     VASKYSLPDL ALYHLETATT AVIQGSLLGS GFDDIGPWNS IMEELADRSR QHYRSLIYEE
     PDFLDFFLSV TPIQEISQLQ ISSRPARRQG GKKDLSSLRA IPWVFSWTQT RFLLPAWYGV
     GTALKGFLDE ETERNREHNL KLLRYFYWKW PFFRMVVSKV EMTLAKVDLQ IAHHYLKELA
     NSEDYDRFER IFKQIADEYY LASELIRLIT DHEKLLDGDP DLQRSVQLRN RTIVPLGFLQ
     VSLLKRLREY SNQSASGVIH FRYSKEELLQ GALLTLNGIA AGMRNTG
//