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Database: UniProt/TrEMBL
Entry: V5V5B1_9CYAN
LinkDB: V5V5B1_9CYAN
Original site: V5V5B1_9CYAN 
ID   V5V5B1_9CYAN            Unreviewed;      1011 AA.
AC   V5V5B1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   07-JUN-2017, entry version 28.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=pepC {ECO:0000313|EMBL:AHB88551.1};
GN   Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=NK55_06230 {ECO:0000313|EMBL:AHB88551.1};
OS   Thermosynechococcus sp. NK55a.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=1394889 {ECO:0000313|EMBL:AHB88551.1, ECO:0000313|Proteomes:UP000018741};
RN   [1] {ECO:0000313|EMBL:AHB88551.1, ECO:0000313|Proteomes:UP000018741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NK55 {ECO:0000313|EMBL:AHB88551.1};
RX   PubMed=24482507;
RA   Stolyar S., Liu Z., Thiel V., Tomsho L.P., Pinel N., Nelson W.C.,
RA   Lindemann S.R., Romine M.F., Haruta S., Schuster S.C., Bryant D.A.,
RA   Fredrickson J.K.;
RT   "Genome Sequence of the Thermophilic Cyanobacterium
RT   Thermosynechococcus sp. Strain NK55a.";
RL   Genome Announc. 2:e01060-13(2014).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP006735; AHB88551.1; -; Genomic_DNA.
DR   RefSeq; WP_024124946.1; NC_023033.1.
DR   EnsemblBacteria; AHB88551; AHB88551; NK55_06230.
DR   KEGG; thn:NK55_06230; -.
DR   PATRIC; fig|1394889.3.peg.1303; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000018741; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018741};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AHB88551.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AHB88551.1}.
FT   ACT_SITE    207    207       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    658    658       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1011 AA;  116459 MW;  EB75EB35A763D33D CRC64;
     MTSVLDATNR DRLIESESLA ARTLQERLRL VEEVLVDVLA AESGQELVDL LRRLGALSSP
     EGHVLHAPEG ELLKVIESLE LNQAIRAARA FNLYFQIINI VEQHYEQQYN RERAAQERLR
     RRSVMSEPIS GVSGEGFPLP HNAANATAVR SGPSERLEHS LYEAIPATQQ YGSFAWLFPR
     LQMLNVPPRH IQKLLDQLDI KLVFTAHPTE IVRQTIRDKQ RRVARLLEQL DVLEGASAHL
     TDWNAQTLRA QLMEEIRLWW RTDELHQFKP EVLDEVEYTL HYFKEVIFAV IPKLYRRLEQ
     SLHETFPTLE PPRHNFCRFG SWVGGDRDGN PYVKPEVTWQ TACYQRNLVL EEYIKSVERL
     INLLSLSLHW CDVLPDLLDS LEQDQRQLPS IYDQYAVRYR QEPYRLKLAY VLKRLQNTRD
     RNRALQTYCI RRHEAEELNN GQFYCHGEEF LAELLLIQRN LKETGLACRE LDDLICQVQV
     FGFNLAALDI RQESTCHAEA LNEITAYLGI LPCPYTELSE TERTRWLLSE LSTRRPLIPG
     ELPFSDRTNE IIETFRMVRQ LQQEFGTDLC NTYIISMSHE VSDLLEVLLF AKEAGLFDPA
     TGASTLQAIP LFETVEDLKH APAVLTQLFS LPFCRSYLGS NSTPFLQEVM LGYSDSNKDS
     GFLSSNWEIY KAQQQLQKIA ENFGFQLRIF HGRGGSVGRG GGPAYAAILA QPAQTIKGRI
     KITEQGEVLA SKYSLPELAL FNLETVATAV IQASLLRSSI DEIEPWHEIM EELATRSRQC
     YRHLIYEQPE FIEFFNEVTP IQEISQLQIS SRPTRRGGKK TLESLRAIPW VFSWTQTRFL
     LPAWYGVGTA LKEFLEEKPA EHLSLLRYFY YKWPFFRMVI SKVEMTLAKV DLEIARYYVQ
     ELSQPQNREA FFRLYDQIAQ EHRLTTELVL TITGHERLLD GDPALQRSVQ LRNRTIVPLG
     FLQVSLLKRL RQHNSQTTSG AILRSRYGRG ELLRGALLTI NGIAAGMRNT G
//
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