ID   B2J5N4_NOSP7            Unreviewed;      1037 AA.
AC   B2J5N4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=Npun_F5459 {ECO:0000313|EMBL:ACC83766.1};
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC83766.1, ECO:0000313|Proteomes:UP000001191};
RN   [1] {ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACC83766.1, ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX   PubMed=23463784; DOI=10.1104/pp.112.213116;
RA   Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT   "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT   Cyanobacterium-Plant Symbiosis.";
RL   Plant Physiol. 161:1984-1992(2013).
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; CP001037; ACC83766.1; -; Genomic_DNA.
DR   RefSeq; WP_012411712.1; NC_010628.1.
DR   AlphaFoldDB; B2J5N4; -.
DR   STRING; 63737.Npun_F5459; -.
DR   EnsemblBacteria; ACC83766; ACC83766; Npun_F5459.
DR   KEGG; npu:Npun_F5459; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; B2J5N4; -.
DR   Proteomes; UP000001191; 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:ACC83766.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001191}.
FT   REGION          109..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        683
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1037 AA;  118418 MW;  199A24903B067C9B CRC64;
     MGSLLYSSSQ TADIYPVSEL FLRHRLQVVE ELWESVLRQE CGQNMVDLLR QLRDLCSPEG
     QATNDQASSA VKLIEQLNIN EAIRAARAFA LYFQLINIIE QEYEQRQQLS RYEAETEPTD
     SERASNVNYS SNQREDDAPV SKGIAAELLA KNYLEKAQVK PKGTFAALFP YLFKQNVPPQ
     QIQRLIAHLD VRLVFTAHPT EIVRHTIRDK QRQVVQLLQK LDTLENHAGG TGGGYAWEAA
     DVREQLLEEI RLWWRTDELH QFKPTVLDEV DYALHYFQEV LFDGIPQLYK RFKHTLSNTF
     PWLEPPSKNF CSFGSWVGSD RDGNPSVTPE VTWQTACYQR KMVLGRYIQS VKNLIELLSV
     SMHWSDVLPD LLESLELDQS QLSEVYDALA LRYRQEPYRL KLAYVLKRLE NTRDRNLALY
     NRETPKNQDS PLYRSGDDFL AELRMIQRNL TETGLSCRDL ENLICQVEIF GFNLTQLDIR
     QESSRHADAL NEILQYLQIL PQPYNELSEE QKVAWLTGEL QTRRPLIPAE LPFSEKTNDV
     IETFRVVRSL QQEFGLNICQ TYIISMCRDV SDVLEVLLLA KEARLFDPAI AVGTIQVVPL
     FETVEDLQRS RSVMRKLFEL PLYRALLAGG YEQTKTESVV VDENSSSLAS PAPPASPASP
     APSPSPLTPN LQEVMLGYSD SNKDSGFLSS NWEIHKAQKS LQQIAEGYDI NLRIFHGRGG
     SVGRGGGPAY EAILAQPGHS INGRIKITEQ GEVLASKYSL LDLALYHMET ITTAVIQASL
     LRTGFDDIEP WNEIMEELAA RSRQHYRALI YEQPDFVDFF HQVTPIEEIS QLQISSRPAR
     RPSGKKDLSS LRAIPWVFSW TQTRFLLPSW YGVGTALQEF LNAEPEEHLK LMRYFYVKWP
     FFKMVISKAE MTLAKVDMQM AHHYVQELSQ SEDQLRFAKV FDQIASEFYL TRDLVLKITD
     HNQLLDGDPV LQRSVQLRNG TIVPLGFIQV SLLKRLRQSM NTNATSGVIH SRYSKGELLR
     GALLTINGIA AGMRNTG
//