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Database: UniProt/TrEMBL
Entry: A0A0G3M3R6_9FLAO
LinkDB: A0A0G3M3R6_9FLAO
Original site: A0A0G3M3R6_9FLAO 
ID   A0A0G3M3R6_9FLAO        Unreviewed;       844 AA.
AC   A0A0G3M3R6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   20-DEC-2017, entry version 15.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=OK18_15490 {ECO:0000313|EMBL:AKK73821.1};
OS   Chryseobacterium gallinarum.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Chryseobacterium.
OX   NCBI_TaxID=1324352 {ECO:0000313|EMBL:AKK73821.1, ECO:0000313|Proteomes:UP000035213};
RN   [1] {ECO:0000313|EMBL:AKK73821.1, ECO:0000313|Proteomes:UP000035213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27622 {ECO:0000313|EMBL:AKK73821.1,
RC   ECO:0000313|Proteomes:UP000035213};
RA   Park G.-S., Hong S.-J., Jung B.K., Khan A.R., Kwak Y., Shin J.-H.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP009928; AKK73821.1; -; Genomic_DNA.
DR   RefSeq; WP_053328580.1; NZ_CP009928.1.
DR   EnsemblBacteria; AKK73821; AKK73821; OK18_15490.
DR   GeneID; 31908795; -.
DR   KEGG; cgn:OK18_15490; -.
DR   PATRIC; fig|1324352.5.peg.3230; -.
DR   KO; K01595; -.
DR   Proteomes; UP000035213; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|SAAS:SAAS00946757};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035213};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AKK73821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035213}.
FT   COILED      609    629       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   844 AA;  97384 MW;  71AC539942E2E2D8 CRC64;
     MIHDQRAEKF RQIVENKFQI YNSLFMSLPY DKMTNIGMLL PFLYEESRTG YEAGKTPEII
     VEEFFKNHTD LETEEQKLEL LFKIIQYIER QVVLFDSIED AAFPNLHSES DNGTVTNLFE
     RSFQDHKLEK VREKLKDFSV KVVFTAHPTQ FYPSSVQRII QDLRGAITSD SVTQIDMLLQ
     QLGKTPFVNK EKPTPIDEAL SIISYLRYVY YDTIGELFTK IKKTFGNGHF HLHEDIIQLG
     FWPGGDRDGN PFVTADVTKR VAEELRSAIL KSYYSHLKFI RRRLSFRGVS EILTQLSEEL
     YAAIFNGKSI TAEDILAKAD EAENILIHEH NSLFLDLLTN FRDRVRIFGT HFATLDIRQD
     SRIHQKAIDE VFARLYGNEE ADPQQKFTRL IQVSEKINPD DFEDIVKDTL LTVSQVSEIQ
     NVNGLRGMNR YIISNSDAVK DVMNVYAFFK VCGYKDEEIN MDIVPLFETM EGLANAENVM
     NELYQNPVYK KHIERRGNQQ TIMLGFSDGT KDGGYLKANW EIYKAKELLT KLSEQHHIKV
     IFFDGRGGPP ARGGGKTHDF YASQGKTIAN NKIELTIQGQ TITSIFGNKE QAKYNFEQLL
     TAGVENDVFK NAKKELTEKE RKLIAELAEI SYKKYADLKA HPMFVPYLQE MSTLEYYGKT
     NIGSRPSKRG NGSELKFEDL RAIPFVGSWS QLKQNVPGFF GFGYAMQQMK EQGRFEEVRE
     LYKGSDFFKT LVLNSMMSMN KSYFPLTYYI KNNPKFGTFW NILFDEYELS KDIMLELTGF
     KMLQEEDPLS RKSVKIREKI VLPLLSIQQY ALMKIQKGEG DKGAYEKLVT RSLFGNINAS
     RNSA
//
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