ID A0A0S3U0E0_9CYAN Unreviewed; 1014 AA.
AC A0A0S3U0E0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=LEP3755_14800 {ECO:0000313|EMBL:BAU10987.1};
OS Leptolyngbya sp. NIES-3755.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1752064 {ECO:0000313|EMBL:BAU10987.1, ECO:0000313|Proteomes:UP000062150};
RN [1] {ECO:0000313|EMBL:BAU10987.1, ECO:0000313|Proteomes:UP000062150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3755 {ECO:0000313|EMBL:BAU10987.1,
RC ECO:0000313|Proteomes:UP000062150};
RA Hirose Y.;
RT "Complete genome sequence of Leptolyngbya sp. NIES-3755.";
RL Submitted (DEC-2015) 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,
CC ECO:0000256|HAMAP-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; AP017308; BAU10987.1; -; Genomic_DNA.
DR RefSeq; WP_068382253.1; NZ_AP017308.1.
DR AlphaFoldDB; A0A0S3U0E0; -.
DR STRING; 1752064.LEP3755_14800; -.
DR KEGG; len:LEP3755_14800; -.
DR PATRIC; fig|1752064.3.peg.1537; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000062150; 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:BAU10987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062150}.
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 662
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1014 AA; 116699 MW; 80E577BE1CD46F5A CRC64;
MSSTRPSSDE FSTSLTTASE DVTAMMSDLF LRHRLRIVED LWEAVLRQEC GQELVDLLNQ
LRRMCSPEGQ ATTFTGSEVL QVVEKLDLNE AIRAARAFAL YFQLINIVEQ HYEQRDQQLQ
YRMAREGHGQ PDPKHERQAY ATEEDAGRPE ADFLERSLHE AASRREIGTF HWLFPRLKQL
NVPPQLIQKL INQLDVWLVF TAHPTEIVRH TIRDKQRRIA KILRQLDSVE DSLKAIGLSS
SWEADSLRDQ LTEEIRLWWR TDELHQFKPT VLDEVDHALH YFREVIFDAI PHLYQRLEEA
VHGSFPKMQM PRRNFCQFGS WVGADRDGNP SVTPQVTWQT ACYQRRLVLE RYVNSIQSLS
ELLSLSLHWS DVLPDLLESL EQEQQRMPEV YDRLSIRFRQ EPYRLKLAYI CKRLENTLER
NQILSNIDGL QQEMPEYDET KIYRSGDDFL TELRLIQSNL AATGLSCRDL DHLICQVEIF
GFNLAHLDIR QESPRHSETM NEVVEYLQVL PKAYNDMSEE ERCQWLISEL KTRRPLIPSE
LPFSDRTREA IATFRMVRKL QQEFGIDICR TYIISMSHDV SDLLEVLLFA KEAGLYDPAT
GFGTIQVVPL FETVEDLQKA PGIMRGVFDL PFYKALLAGG FESIGVTTAL QEVMLGYSDS
NKDSGFLSSN WEIHKAQQAL QSIADEHGVV LRIFHGRGGS VGRGGGPAYE AILAQPGHSV
NGRIKITEQG EVLASKYSLP ELALYNLETV TTAVIQGSLL QNKFDEIAPW QQVMEELAAR
SRKHYRSLIY EQPDFIDFFH QVTPIEEISQ LQISSRPARR GGKKDLASLR AIPWVFSWTQ
SRFLLPSWYG VGTALQGFLD EAPEKHMQLL RHFYFKWPFF KMAISRVEMT LSKVDLQIAS
HYVDELTQPE DRERFAPVFE QIRNEYLLTR ELVLTITGHN RLLDGDPELQ RSVQLRNGTI
VPLGFLQVSL LKRLRQHKTL AASGVVRSRY SKGELLRGAL LTINGIAAGM RNTG
//