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Database: UniProt
Entry: X5F6B6_NEIME
LinkDB: X5F6B6_NEIME
Original site: X5F6B6_NEIME 
ID   X5F6B6_NEIME            Unreviewed;       923 AA.
AC   X5F6B6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ECO:0000313|EMBL:AHW74708.1};
GN   ORFNames=NMA510612_0397 {ECO:0000313|EMBL:AHW74708.1};
OS   Neisseria meningitidis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487 {ECO:0000313|EMBL:AHW74708.1, ECO:0000313|Proteomes:UP000023582};
RN   [1] {ECO:0000313|EMBL:AHW74708.1, ECO:0000313|Proteomes:UP000023582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RX   PubMed=24812217;
RA   Zhang Y., Yang J., Xu L., Zhu Y., Liu B., Shao Z., Zhang X., Jin Q.;
RT   "Complete Genome Sequence of Neisseria meningitidis Serogroup A Strain
RT   NMA510612, Isolated from a Patient with Bacterial Meningitis in China.";
RL   Genome Announc. 2:e00360-14(2014).
RN   [2] {ECO:0000313|Proteomes:UP000023582}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RA   Zhang X., Zhang Y., Yang J., Zhu Y., Jin Q.;
RT   "Complete Genome Sequence of Neisseria meningitides, serogroup A strain
RT   510612.";
RL   Submitted (FEB-2014) 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}.
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DR   EMBL; CP007524; AHW74708.1; -; Genomic_DNA.
DR   AlphaFoldDB; X5F6B6; -.
DR   KEGG; nmx:NMA510612_0397; -.
DR   PATRIC; fig|487.517.peg.400; -.
DR   Proteomes; UP000023582; Chromosome.
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.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 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:AHW74708.1}.
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   923 AA;  104021 MW;  4FF8B98B81509649 CRC64;
     MNGLARMRHL RYIYSIYGNE RKIMQLHILN NPKDAALAAD AEFLKQSLFN LLHEEASPLV
     VETVKLLSTS DDSAALIEKV LPQLDEQQTH DLTLACGLFA QILNIAEDVH HERRRQIHEE
     AGRGGAEGSL TETVRRLKAG KADGKSVQRQ LDNTSVTAVL TAHPTEVQRQ TVLSFNRRIR
     ALLPQRERCT NADALARLRR EIDTILLGLW QTSETRRHKL SVNDEINNGV SIFPMSFFEA
     LPKLYRKMEH DFQMVYPDVC VPNILKIGGW IGGDRDGNPF VSAETLRFAF RRHADAVFRF
     YRSELDKLYR ELPLSIRRVK VNDDVMALAA LSPDEELART EEPYRRAIAY IMARAMGKAR
     ALGLGMGCKF GFLEPYASAQ EFLDDLKKLQ RSLIDNGSRL LAEGRLADII RSVSVFGFHM
     MPLDLRQHAG KHADVVAELF QHAGLEDYNS LNEEQKQAVL LRELSHQRPL YSPFITYSEH
     TRHELAIFNE ARKIKDEFGE DAVTQSIISN CEQPSDLLAL ALLLKESGLL AVENGKPRSR
     INIVPLFETI EALENACPVM ETMFRLDWYD ALLESCGNIQ EIMLGYSDSN KDGGYVTSSW
     CLYQAELGLV ELFKKYDVRM RLFHGRGGSV GRGGGPSYQA ILAQPAGSVA GQIRITEQGE
     VITAKYADPG NAQRNLETLV AATLEASILP DKKDPDAKLM QDLSDVSFKY YRELITHPDF
     IDYFLQTSPI QEIATLNLGS RPASRKTLAR IQDLRAIPWV FSWMQNRLML PAWYGFGSAV
     ETLCEGNPDT LAALREHAQS NPFFQAMLSN MEQVMAKTDI TLAENYAGLS ESPDKAKVIF
     GMIKEEYRRS RKALLDLLQT EELLRDNRSL ARSLALRIPY LNALNGLQVA MLKRLRKEPD
     NPHALLMVHL TINGVAQGLR NTG
//
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