CAPP_THEVB
ID CAPP_THEVB Reviewed; 1011 AA.
AC P0A3X5; Q94QB2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppc; OrderedLocusNames=tll1912;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC09464.1; -; Genomic_DNA.
DR RefSeq; NP_682702.1; NC_004113.1.
DR RefSeq; WP_011057749.1; NC_004113.1.
DR AlphaFoldDB; P0A3X5; -.
DR SMR; P0A3X5; -.
DR STRING; 197221.22295638; -.
DR EnsemblBacteria; BAC09464; BAC09464; BAC09464.
DR KEGG; tel:tll1912; -.
DR PATRIC; fig|197221.4.peg.2000; -.
DR eggNOG; COG2352; Bacteria.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000000440; 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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT CHAIN 1..1011
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166640"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 658
FT /evidence="ECO:0000250"
SQ SEQUENCE 1011 AA; 116427 MW; 0A11D4D01FE9E7FE CRC64;
MTSVLDVTNR DRLIESESLA ARTLQERLRL VEEVLVDVLA AESGQELVDL LRRLGALSSP
EGHVLHAPEG ELLKVIESLE LNEAIRAARA FNLYFQIINI VEQHYEQQYN RERAAQEGLR
RRSVMSEPIS GVSGEGFPLP HTAANATDVR SGPSERLEHS LYEAIPATQQ YGSFAWLFPR
LQMLNVPPRH IQKLLDQLDI KLVFTAHPTE IVRQTIRDKQ RRVARLLEQL DVLEGASPHL
TDWNAQTLRA QLMEEIRLWW RTDELHQFKP EVLDEVEYTL HYFKEVIFAV IPKLYRRLEQ
SLHETFPALQ PPRHRFCRFG SWVGGDRDGN PYVKPEVTWQ TACYQRNLVL EEYIKSVERL
INLLSLSLHW CDVLPDLLDS LEQDQRQLPS IYEQYAVRYR QEPYRLKLAY VLKRLQNTRD
RNRALQTYCI RRNEAEELNN GQFYRHGEEF LAELLLIQRN LKETGLACRE LDDLICQVEV
FGFNLAALDI RQESTCHAEA LNEITAYLGI LPCPYTELSE AERTRWLLSE LSTRRPLIPG
ELPFSDRTNE IIETFRMVRQ LQQEFGTDLC NTYIISMSHE VSDLLEVLLF AKEAGLFDPA
TGASTLQAIP LFETVEDLKH APAVLTQLFS LPFCRSYLGS NSTPFLQEVM LGYSDSNKDS
GFLSSNWEIY KAQQQLQKIA ESFGFQLRIF HGRGGSVGRG GGPAYAAILA QPAQTIKGRI
KITEQGEVLA SKYSLPELAL FNLETVATAV IQASLLRSSI DEIEPWHEIM EELATRSRQC
YRHLIYEQPE FIEFFNEVTP IQEISQLQIS SRPTRRGGKK TLESLRAIPW VFSWTQTRFL
LPAWYGVGTA LKEFLEEKPA EHLSLLRYFY YKWPFFRMVI SKVEMTLAKV DLEIARYYVQ
ELSQPQNREA FCRLYDQIAQ EYRLTTELVL TITGHERLLD GDPALQRSVQ LRNRTIVPLG
FLQVSLLKRL RQHNSQTTSG AILRSRYGRG ELLRGALLTI NGIAAGMRNT G