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Database: UniProt/TrEMBL
Entry: A0A0P0F751_AZOBR
LinkDB: A0A0P0F751_AZOBR
Original site: A0A0P0F751_AZOBR 
ID   A0A0P0F751_AZOBR        Unreviewed;       935 AA.
AC   A0A0P0F751;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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   ORFNames=AMK58_27060 {ECO:0000313|EMBL:ALJ39136.1};
OS   Azospirillum brasilense.
OG   Plasmid ABSP7_p3 {ECO:0000313|EMBL:ALJ39136.1,
OG   ECO:0000313|Proteomes:UP000065707}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192 {ECO:0000313|EMBL:ALJ39136.1, ECO:0000313|Proteomes:UP000065707};
RN   [1] {ECO:0000313|EMBL:ALJ39136.1, ECO:0000313|Proteomes:UP000065707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp 7 {ECO:0000313|EMBL:ALJ39136.1,
RC   ECO:0000313|Proteomes:UP000065707};
RC   PLASMID=Plasmid ABSP7_p3 {ECO:0000313|Proteomes:UP000065707};
RA   Millard Andrew;
RL   Submitted (OCT-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, ECO:0000256|SAAS:SAAS00730191}.
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; CP012917; ALJ39136.1; -; Genomic_DNA.
DR   RefSeq; WP_059399685.1; NZ_JPIS01000010.1.
DR   EnsemblBacteria; ALJ39136; ALJ39136; AMK58_27060.
DR   KEGG; abf:AMK58_27060; -.
DR   KO; K01595; -.
DR   Proteomes; UP000065707; Plasmid ABSP7_p3.
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:UP000065707};
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   Plasmid {ECO:0000313|EMBL:ALJ39136.1};
KW   Pyruvate {ECO:0000313|EMBL:ALJ39136.1}.
FT   ACT_SITE    162    162       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    597    597       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   935 AA;  103997 MW;  79B0F6355A5EE56F CRC64;
     MTTHAARHST APANDTETGT DDKDFPLRED IRLLGRLLGD TVREQEGDGV YGVIESVRQA
     SVRFNRDDDD SARREMAEIL NGLPRDTMMS VVRAFSYFLH LANIAEDQHH IRRTRDHAIA
     GSPAREGTLP YALERLEAAG VAPDRLAGVL DIAQVSPVLT AHPTEVQRKS ILALEHKVAS
     LLDTRDRSRL TPEEAEANMD ALQEAILTLW RTRMLRPQRL AVIDEVKNGI SYYTDTFFSE
     LPKLFCRFED LLAKRFPERE WSLPPYFRIG SWIGGDRDGN PFVTAPILRE AMRLQSTAAL
     DHYLTEIHEL GGELPLSELL LGTSPELEEL AKRSPDHSPH RADEPFRRAL TGIYARLAAT
     SRTLDQHEAL RNAVGKGDPY PTSAELLADL EVLAASLKAH GAGRLAAGRL RRLIIAVKTF
     GFHLAPIDLR QNSDVHQRTV AELLAVAGRC ADYAALSEDE RIALLAEEIQ SPRPLHSPYH
     AYSEETAGEL AIFFAARQLR ETYGPAALPN SIISKTDGAS DLLEVALLLK ESGLLRPGAG
     GEPGLGLNIV PLFETIEDLR QAPATMERLF TLPAYRALVT SRGDEQEVML GYSDSNKDGG
     FLTSGWELYK AEIELAKLFD RHGVRMRLFH GRGGSVGRGG GPSYQAILAQ PTGAVSGQIR
     ITEQGEVIAS KYGRPEVGQR NLEVLTAATL EATLLDLENR VEPAESFYAA MERLSELAFG
     AYRGLVYETP GFTQYFRTAT PISEIATLNI GSRPASRTKS DRIEDLRAIP WVFSWAQCRL
     MLPGWYGFGS AVEAWLKEEP DGLALLQRMN RAWPFFKSLL SNMDMVLAKS DLAIASRYAE
     LVEDVELRER IFGRIREEWQ RTRRHLLAIA GHDELLGENP LLARSIRNRF PYMDPLNHVQ
     VELLRRHRAG SSDERVRRGI LMSINGVAAG LRNSG
//
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