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Database: UniProt
Entry: A0A0N0MRB3_9ACTN
LinkDB: A0A0N0MRB3_9ACTN
Original site: A0A0N0MRB3_9ACTN 
ID   A0A0N0MRB3_9ACTN        Unreviewed;       942 AA.
AC   A0A0N0MRB3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
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|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=OK074_4748 {ECO:0000313|EMBL:KPI04221.1};
OS   Actinobacteria bacterium OK074.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI04221.1, ECO:0000313|Proteomes:UP000037991};
RN   [1] {ECO:0000313|EMBL:KPI04221.1, ECO:0000313|Proteomes:UP000037991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK074 {ECO:0000313|EMBL:KPI04221.1,
RC   ECO:0000313|Proteomes:UP000037991};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
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         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI04221.1}.
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DR   EMBL; LJCV01000269; KPI04221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0MRB3; -.
DR   PATRIC; fig|1592327.3.peg.7249; -.
DR   Proteomes; UP000037991; Unassembled WGS sequence.
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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:KPI04221.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        600
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   942 AA;  104077 MW;  E0A0FEAF191087FD CRC64;
     MSSADDTKTT PGAPTASGDP TATTHGQATG TPHGTAPAAP EATSSALRAD IRRLGDLLGE
     TLVRQEGPEL LELVEKVRRL TREDGEAAAE LLRGTELETA AKLVRAFSTY FHLANVTEQV
     HRGRELRARR AAEGGLLART ADRLKDADPD HLRETVQHLN VRPVFTAHPT EAARRSVLNK
     LRRIAALLDT PVIESDRRRY DTRLAENIDL VWQTDELRVV RPEPADEARN AVYYLDELHA
     GAVGDVLEDL TAELERVGVK LPDETRPVTF GTWIGGDRDG NPNVTPQVTW DVLILQHEHG
     INDALDLIDE LRGFLSNSIR YTGATEELLE SLRADLEQLP GISPRYKRLN AEEPYRLKAT
     CIRQKLVNTK QRLAKGTPHE PGRDYLGTAE LLRDLTLIQT SLREHRGGLF ADGRMNRTIR
     TLAAFGLQLA TMDVREHADA HHHALGQLFD RLGEESWRYE DMPREYRHKL LAKELRSRRP
     LAPTPAPLDA AGTKTIGVFE TVKRALAVFG PEVIESYIIS MCQGADDVFA AAVLAREAGL
     IDLHAGWAQI GIVPLLETTD ELKAADTILE DMLSDPSYRR LVALRGDVQE VMLGYSDSSK
     FGGITTSQWE IHRAQRRLRD VAHRYGVRLR LFHGRGGTVG RGGGPSHDAI LAQPWGTLEG
     EIKVTEQGEV ISDKYLIPAL ARENLELTVA ATLQASALHT SPRQSVEALA RWDAAMDVVS
     EAAHSAYRGL VEDPDLPTYF LASTPVDQLA ELHLGSRPSR RPGSGVSLDG LRAIPWVFGW
     TQSRQIVPGW FGVGSGLKAL REAGLDTVLD EMHEQWHFFR NFVSNVEMTL AKTDLRIAQH
     YVDTLVPENL KHVFDAIRTE HELTVAEILR VTGEAELLDA QPVLKQTFTI RDAYLDPISY
     LQVALLKRQR DAATAGVEAD PILARALLLT VNGVAAGLRN TG
//
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