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Database: UniProt/TrEMBL
Entry: A0A0H5PV83_SYNPZ
LinkDB: A0A0H5PV83_SYNPZ
Original site: A0A0H5PV83_SYNPZ 
ID   A0A0H5PV83_SYNPZ        Unreviewed;      1010 AA.
AC   A0A0H5PV83;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CRY93047.1};
GN   ORFNames=SynWH8103_02354 {ECO:0000313|EMBL:CRY93047.1};
OS   Synechococcus sp. (strain WH8103).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=29410 {ECO:0000313|EMBL:CRY93047.1, ECO:0000313|Proteomes:UP000036508};
RN   [1] {ECO:0000313|EMBL:CRY93047.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WH 8103 {ECO:0000313|EMBL:CRY93047.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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; LN847356; CRY93047.1; -; Genomic_DNA.
DR   EnsemblBacteria; CRY93047; CRY93047; SynWH8103_02354.
DR   KEGG; synw:SynWH8103_02354; -.
DR   KO; K01595; -.
DR   Proteomes; UP000036508; Chromosome 1.
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   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 {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036508};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CRY93047.1}.
FT   ACT_SITE    195    195       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    652    652       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1010 AA;  114474 MW;  BA7E0C2F5083B11E CRC64;
     MINRSPETSG ASMPQSTAHV PDGEQPRASG GSPGAGRLLQ HRLELVEDLW QTVLRSECPP
     EQSERLLRLK QLSDPVALEG RDGESSSEAI VELIRSMDLS EAIAAARAFS LYFQLINILE
     QRIEEDSYLD SLRPSRSQDD ETAAPFDPFA PPLASQTDPA TFGEVFERLR RMNVPPAQVE
     TLLRELDIRL VFTAHPTEIV RHTVRHKQRK VASLLQRLQS EPALPRYDEE ELRRQLEEEI
     RLWWRTDELH QFKPTVLDEV DSTLHYFQQV LFEAMPQLRR RLVSSLSRHY PDVQFPQASF
     CTFGSWVGSD RDGNPSVTPE ITWRTACYQR QLMLELYIGS VQSLRNQLSI SMQWSQVAPP
     LLESLEMDRL RFPEIYERRA ARYRLEPYRL KLSYILERLE LTLQRNHQMS EAGWQSPPEP
     AATAPTDGIP GHEALHYTAI DQFRSDLELI RNSLVSTELS CEQLDTLLNQ VHIFGFSLAS
     LDIRQESTRH SDAIDELTTH LQLPKAYGAM EESERVAWLL EELQTRRPLI PAAVEWSEAT
     AQTFAVFQML HRLQQEFGQR ICHSYVISMS HTASDLLEVM LLAKEIGLVD PQAGKASLLV
     VPLFETVEDL QRAPAVMDGL FQTPIYRNLL PSVGVQRQPL QELMLGYSDS NKDSGFLSSN
     WEIHQAQIAL QTLASSHGVA LRLFHGRGGS VSRGGGPAYQ AILAQPSGTL QGRIKITEQG
     EVLASKYGLP ELALYNLETV TTAVVQNSLV TNQLDATPSW NQLMSRVAKR SREHYRALVH
     DNPDLVAFFQ QVTPIEEISK LQISSRPARR KTGARDLSSL RAIPWVFGWT QSRFLLPSWF
     GVGTALAEEV NDDPEQLDLL RRLHQRWPFF RMLISKVEMT LSKVDLDLAH HYMSSLGNPE
     QRDAFEGIFK VIADEYGRTL KLVLEITGQS RLLGADQNLQ LSVDLRNRTI VPLGFLQVAL
     LRRLRDQNRQ PPMSESPGTP EDRRTYSRSE LLRGALLTLN GIAAGMRNTG
//
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