ID   A2CBZ9_PROM3            Unreviewed;      1002 AA.
AC   A2CBZ9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   ECO:0000313|EMBL:ABM79009.1};
GN   OrderedLocusNames=P9303_22741 {ECO:0000313|EMBL:ABM79009.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM79009.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM79009.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM79009.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM79009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2CBZ9; -.
DR   STRING; 59922.P9303_22741; -.
DR   KEGG; pmf:P9303_22741; -.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000002274; 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:ABM79009.1}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        648
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1002 AA;  113693 MW;  7CD7A46474095878 CRC64;
     MAKPESTSAS MQQSSAQKPD CDQPRAIGEG QQAGRLLQNR LELVEDLWQT VLRSECPPDQ
     AERLLRLKQL SEPLALEGAD ENSASTAIVL LIKEMDLAEA ITAARAFSLY FQLVNILEQR
     IEEDSYLASM SSGKENNRQD KPYDPFAPPL ATQTDPATFS ELFERLRLLN VPPAQLETLL
     QEMDIRLVFT AHPTEIVRHT VRHKQRKVAN LLQQLQSDPT KSSSEKESLR LQLEEEIRLW
     WRTDELHQFK PSVLDEVDYA LHYFQQVLFD AMPQLRRRLI TAMAESYPDV HIPQAAFCTF
     GSWVGSDRDG NPSVTPEITW RTACYQRQLM LERYVNAVQK LRDQLSISMQ WSQVSTPLLE
     SLEMDRLRFP EVYEERAARY RLEPYRLKLS YTLERLKLTQ ERNQQLAEAG WQTPPEGLNP
     SLNLINAGEA LHYKSVAEFR SDLELIRNSL VSTDLSCEPL DTLLNQVHIF AFSLASLDIR
     QESTRHSDAL DELTRYLNLP KAYGDMAENE RVQWLIEELQ TRRPLIPSAV IWSPSTAETV
     AVFRMLHRLQ EEFGSRICRT YVISMSHTVS DLLEVLLLAK EAGLVDPAAG HAELLVVPLF
     ETVEDLQRAP AVMEALLSSP VYRNLLPRVS EQVQPLQELM LGYSDSNKDS GFLSSNWEIH
     QAQIALQDLA NRQGVALRLF HGRGGSVGRG GGPAYQAILA QPSGTVRGRI KITEQGEVLA
     SKYSLPELAL YNLETFTTAV LQNSLVTNQL DATPSWNQLM TRLAGRSREH YRALVHNNPD
     LVAFFQQVTP IEEISKLQIS SRPARRKSGA KDLSSLRAIP WVFGWTQSRF LLPSWFGVGT
     ALAAEVESDA DQLDLLRRLH QRWPFFRMLI SKVEMTLSKV DLDLAHHYMT SLGSEDYREA
     FNRIFEIIET EYSLTRRLVL NITGQPRLLG ADPALQQSVD LRNRTIVPLG FLQVALLRKL
     RDQNRQPPMN EAGDGRTYSR SELLRGALLT INGIAAGMRN TG
//