ID W1UG54_9STRE Unreviewed; 901 AA.
AC W1UG54;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=Q617_SPSC00389G0016 {ECO:0000313|EMBL:ETI92450.1};
OS Streptococcus sp. DORA_10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1403937 {ECO:0000313|EMBL:ETI92450.1, ECO:0000313|Proteomes:UP000018865};
RN [1] {ECO:0000313|EMBL:ETI92450.1, ECO:0000313|Proteomes:UP000018865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_10 {ECO:0000313|Proteomes:UP000018865};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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:ETI92450.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZMH01000389; ETI92450.1; -; Genomic_DNA.
DR PATRIC; fig|1403937.3.peg.1524; -.
DR Proteomes; UP000018865; 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:ETI92450.1}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 564
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 901 AA; 103651 MW; 8098C73B4A2071A8 CRC64;
MSLQKLENYS NKAVIQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST QEDYQGLNQL
VTSLTNDEMA YISRYFSILP LLINISEDVD LAYEINHQNN IXXXXQDYLG KLSATIKMVA
EKENAVEILE HLNVVPVLTA HPTQVQRKSM LDLTNHIHTL LRKYRDVKLG LINKEKWHND
LRRYIEIIMQ TDMIREKKLK VTNEITNVME YYNSSFLKAV PHLTAEYKRL AKKHGLELKH
PKPITMGMWI GGDRDGNPFV TADTLKQSAM TQCEVIMNYY DEKIYQLYRE FSLSTSIVNV
SKQVREMARQ SKDNSIYREK ELYRRALFDI QSKIQATKTY LIEDKEVGAR YETANDFYKD
LITIRDSLLE NKGEALISGD FVELIQAVEI FGFYLASIDM RQDSSVHEAC VAELLKSAGI
HSHYSELGEE EKCQLLLKEL EEDPRILSAT HVEKSELLEK ELAIFKAARK LKDKLGDDVI
RQTIISHATS VSDMLELAIL LKEVGLVDKE RARVQIVPLF ETIEDLDHSE ETMREYLSLP
LAKKWIASRN NYQEIMLGYS DSNKDGGYLS SCWTLYKAQQ QLTAIGDEFG VKVTFFHGRG
GTVGRGGGPT YEAITSQPLK SIKDRIRLTE QGEVIGNKYG NKDAAYYNLE MLVSAAINRM
ITQKKSDTNT SNRYEAIMDQ VVDRSYDIYR DLVFGNDHFY DYFFESSPIK AISSFNIGSR
PAARKTITEI GGLRAIPWVF SWSQSRVMFP GWYGVGSSFK EFIDKNPENI AILRDMYQNW
PFFQSLLSNV DMVLSKSNMN IAFEYAKLCE DEEVKAIYET ILNEWQVTKE VILAIEGYDE
LLAENPYLKA SLDYRMPYFN ILNYIQLELI KRQRRGELSS DQEKLIHTTI NGIATGLRNS
G
//
