ID A0A1Z4RKQ2_9CHRO Unreviewed; 1023 AA.
AC A0A1Z4RKQ2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:BAZ43048.1};
GN ORFNames=NIES4102_00440 {ECO:0000313|EMBL:BAZ43048.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ43048.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ43048.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ43048.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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; AP018281; BAZ43048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RKQ2; -.
DR KEGG; chon:NIES4102_00440; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000217698; 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:BAZ43048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217698}.
FT ACT_SITE 194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 668
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1023 AA; 117029 MW; E98C5D9B1BA08A05 CRC64;
MSSVVQSSIA KQEEIGVIGT SHLLLRHRQK LIEDLWKSVL RSECGQEMLD LLQQMRALSS
AEGQVTDTFG QSSVPQLIED LDINDAIQAA RAFALYFQLT NIIEQHYESR EQKLSRRVTH
PITNVENHSN GSQNGSQVVP INNGDLQIEP SISSENKAGL FHWLFPYLKE INMPPLMLQR
LLDQLDIRLV FTAHPTEIVR HTIRKKQRRI SQILEQLDVA EEAMREMGLT DSWETNEATS
QLTEEIRLWW RTDELHQFKP KVLDEVDYSL HYFQEVLFDV IPQLASRLKQ SLTTSFPNLV
APTHNFCYFG SWVGADRDGN PFVTPQVTWE TACYQRSIVI EKYLKSIEQL RELLSLSLHW
SDVGQELLDS LEQDQQQMPE IYEKLSIRYR QEPYRLKLAY IAQRLQNTLE RNQTLASVAG
RQAISEIKID NIYTSGEEFV AELKLMQSSL EATSLQCREL DNLICQAEVY GFTLVELDFR
QDSSRHAEAI AEITAYLQVL PKPYNELSET EKTAWLIQEL KTRRPLIPAE MPFSPETCET
IETFRILRLL QQEFGRGICQ TYIISMTNFV SDVLEVLLLS QEAGLYDPAT CHTSIRIVPL
FETVEDLKRA PQVMQELFEL PLYRAALAGG YKHVATIKEQ NTSTETSTIP LKPTDLQEVM
LGYSDSNKDS GFLSSNWEIH KAQRALQKVA SKFDISLRIF HGRGGSVGRG GGPAYSAILA
QPTDTIKGRI KITEQGEVLA SKYSLPELAL YHLETMTTAV IQASLLGSGF DRVEPWNQIM
EELSARSRSV YRALIYEQPD FVDFFHSVTP VDVISQLQIG SRPSKRPAKG NDNKKKDMSS
LRAIPWVFSW TQSRFLLPAW YGVGSALQGF LDQEPQKNLD LLQYFYVKWP FFRVVISKVE
MTLAKVDLQI AEHYVKELSQ PEDLERFQKL FAQISQEYYL TKDLILKING QKKLLDGNPE
LQRSVQLRNG TIVPLGFLQV ALIKRLRQYD KSQVLHFRFS KEELLRGAML TINGIAAGMR
NTG
//
