ID I0SE08_STRAP Unreviewed; 899 AA.
AC I0SE08;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:EID21611.1};
GN ORFNames=HMPREF1043_1403 {ECO:0000313|EMBL:EID21611.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID21611.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID21611.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID21611.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) 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:EID21611.1}.
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DR EMBL; AICP01000040; EID21611.1; -; Genomic_DNA.
DR RefSeq; WP_003036032.1; NZ_AICP01000040.1.
DR AlphaFoldDB; I0SE08; -.
DR PATRIC; fig|1095729.3.peg.1181; -.
DR Proteomes; UP000003245; 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; 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; 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:EID21611.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT ACT_SITE 561
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 899 AA; 103735 MW; 74F6FCB3CA2B1EC3 CRC64;
MSLQKLENYN NKEVIKEEVT ILTDLLEEVT KNMLSPETFE KIIALKELAA AGNYEGLNEI
VQSLSNKEMS YISRYFSILP LLINISEDVD LAFEINYQNN VGQDYLGKLS TTIDLVAEKE
NAAEILEHLN VVPVLTAHPT QVQRTTMLDL TNHIHVLLRK YRDVRMGLLN EQKWHNNLRR
YIEIIMRTDM IREKKLKVTN EITNVMEYYN SSFLQAVTNL TEEYKRLAKQ HGIDLKNPTP
ITMGMWIGGD RDGNPYVTAE TLKKSALTQC EVIMNYYDTK VANLYREFSL STGIVKVSEA
VQEMAYLSED NSIYREKELY RRAFYYIQTK LKNTKTYFID QIKTEPHYHK IEEFKHDLLA
IKQSLLENKG EAMISGEFTE LLQAVEVFGF YLASIDMRQD SSVHEACVAE LLASAGIVEH
YSELSEDEKC HVLLNELLYD PRILSATHAK KSALLQKELE IFQTARELKD KLGDAVIKQT
IISHATSVSD LLELAVMHKE VGLIDKEFAR VQIVPLFETI EDLDNSYDTM KKYLSLPIAQ
KWIASNNNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKI TFFHGRGGTV
GRGGGPTYEA ITSQPLRSIN DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SATINRMITK
KKSDTSTSNR YEHIMDQVVE RSYQIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI DENPKENLAF LRKMYKNWPF
FQSLLSNVDM VLSKSNMNIA FEYAKLCEDE KVQEIYYTIL DEWQLTKNVI LAIEDYDELL
EENPYLRDSL DYRMRYFNIL NYIQLELIKR QRRGELSPDE ERLIHVTING IATGLRNSG
//
