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Database: UniProt
Entry: A0A1E3L9W1_9BACL
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ID   A0A1E3L9W1_9BACL        Unreviewed;       931 AA.
AC   A0A1E3L9W1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=PTI45_00214 {ECO:0000313|EMBL:ODP30493.1};
OS   Paenibacillus nuruki.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP30493.1, ECO:0000313|Proteomes:UP000094578};
RN   [1] {ECO:0000313|EMBL:ODP30493.1, ECO:0000313|Proteomes:UP000094578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP30493.1,
RC   ECO:0000313|Proteomes:UP000094578};
RA   Kim S.-J.;
RT   "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT   traditional nuruk.";
RL   Submitted (AUG-2016) 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:ODP30493.1}.
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DR   EMBL; MDER01000002; ODP30493.1; -; Genomic_DNA.
DR   RefSeq; WP_069325698.1; NZ_OY725677.1.
DR   AlphaFoldDB; A0A1E3L9W1; -.
DR   STRING; 1886670.PTI45_00214; -.
DR   PATRIC; fig|1886670.3.peg.215; -.
DR   Proteomes; UP000094578; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:ODP30493.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094578}.
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   931 AA;  107095 MW;  6E4A5934CD23F3D6 CRC64;
     MSELTVNASK NHSNNLLRRD VRFLGNILGE VLVHQGGQEL LDIVEKIREL SKSLRAVALP
     EVFEEFKTLI KNLDSDNRHQ VVRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETIQPGSM
     ESAVQELKEQ NFTADEVEAI LADLSLELVM TAHPTEAMRR AILDIHKRIS EDVTLLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETLFD VLPELYQELE
     RSLSKYYPEH EWHVPSFLRF GSWIGGDRDG NPSVTADVTW KTLQMQRRLA IREYQRILTD
     LMKSLSFSTT IIDVSEELLS SIQKDRLHVT IDKKFSWNNE NEPYRIKIAY MLRKLNNILD
     ESKKGTAESY SHMGELLEDL RVIDQSLRHH YADYVANTYV KKLIRQVELF GFHTATLDIR
     QHSQEHENAL TEILASMKIV EDYSKLSEEE KIELLGKLLT DPRPLTSTYL NYSESTEECL
     AVYRTIFKAQ KEFGTNCISS YLISMTQGAS DILEVMIFAK EVGLFRQDPD GTVHSTLQAV
     PLFETIDDLH AAPQIMRQVL NLPAYRQSVA AMNNLQEIML GYSDSNKDGG VVTANWELRL
     ALNEITAMGA EYDIKLKFFH GRGGALGRGG MSLNRSILAQ PPHTVGGGIK ITEQGEVISS
     RYSLQGIAYR SLEQATSALI TSAIIAKVGE PEGENNKKWE QIMEDISEVS LHKYQDLIFR
     DESFMSFFKG STPLPEVGEL NIGSRPSKRK NSDRFEDLRA IPWVFAWTQS RYLLPAWYAA
     GTGIQHFYQD KEENMAVLQE MYKEFPFFTT LVDTLQMAIA KADLIIAKEY AGMYKDEEQR
     ERIFGLIQEE FNRTRDLVLK ITHQQDILDN VPVIQESVRL RNPYVDPLSY LQVQLLNELR
     ELREQDEDNP ELLREVLLTI NGIAAGLRNT G
//
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