ID C6SGK2_NEIME Unreviewed; 821 AA.
AC C6SGK2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 03-MAY-2023, entry version 60.
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:CBA04047.1};
GN ORFNames=NMW_0068 {ECO:0000313|EMBL:CBA04047.1};
OS Neisseria meningitidis alpha275.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=295996 {ECO:0000313|EMBL:CBA04047.1};
RN [1] {ECO:0000313|EMBL:CBA04047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha275 {ECO:0000313|EMBL:CBA04047.1};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889138; CBA04047.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SGK2; -.
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:CBA04047.1}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 489
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 821 AA; 92501 MW; 84F352A7E854BF94 CRC64;
MNIAEDVHHE RRRQIHEEAG RGGAEGSLTE TVRRLKAGKA DGKSVQRQLD NTSVTAVLTA
HPTEVQRQTV LNFNRRIRAL LPQRERCTNA DALARLRREI DTILLGLWQT SETRRHKLSV
NDEINNGVSI FPMSFFEALP KLYRKMEHDF QTAYPDVRVP NILKIGGWIG GDRDGNPFVS
AETLRFAFRR HADAVFRFYR GELDKLYREL PLSIRRVKVN DDVMALAALS PDEELARTEE
PYRRAIAYIM ARAMGKARAL GLGMGCKFGF LEPYASAQEF LDDLKKLQRS LIDNGSRLLA
EGRLADLIRS VSVFGFHMMP LDLRQHAGKH ADVVAELFQH AGLEDYNSLN EEQKQAALLR
ELSHQRPLYS PFITYSDHTR HELAIFNEAR KIKDEFGEDA VTQSIISNCE QPSDLLALAL
LLKESGLLAV ENGKPRSRIN IVPLFETIEA LENACPVMET MFRLDWYDAL LESCGNIQEI
MLGYSDSNKD GGYVTSSWCL YQAELGLVEL FKKYDVRMRL FHGRGGSVGR GGGPSYQAIL
AQPAGSVAGQ IRITEQGEVI TAKYADPGNA QRNLETLVAA TLEASILPDK KDPDAKLMQA
LSDVSFKYYR ELITHPDFID YFLQTSPIQE IATLNLGSRP ASRKTLARIQ DLRAIPWVFS
WMQNRLMLPA WYGFGSAVET LCEDKPETLA ALREHAQSNP FFQAMLSNME QVMAKTDITL
AENYAGLSES PEKAAVIFGM IKEEYQRSRK ALLDLLQTEE LLRDNRSLAR SLALRIPYLN
ALNGLQVAML KRLRKEPDNP HALLMVHLTI NGVAQGLRNT G
//
