ID V8IBC9_STRMT Unreviewed; 898 AA.
AC V8IBC9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=U758_04800 {ECO:0000313|EMBL:ETD98369.1};
OS Streptococcus mitis 27/7.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1415766 {ECO:0000313|EMBL:ETD98369.1, ECO:0000313|Proteomes:UP000018726};
RN [1] {ECO:0000313|EMBL:ETD98369.1, ECO:0000313|Proteomes:UP000018726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=27/7 {ECO:0000313|EMBL:ETD98369.1,
RC ECO:0000313|Proteomes:UP000018726};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Karpova I.Y.,
RA Semashko T.A., Larin A.K., Ischenko D.S., Savinova T.A., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RT "Genome sequencing of Streptococcus mitis strains.";
RL Submitted (NOV-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:ETD98369.1}.
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DR EMBL; AYRS01000005; ETD98369.1; -; Genomic_DNA.
DR RefSeq; WP_023947212.1; NZ_AYRS01000005.1.
DR AlphaFoldDB; V8IBC9; -.
DR PATRIC; fig|1415766.3.peg.920; -.
DR Proteomes; UP000018726; 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:ETD98369.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 561
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 898 AA; 103254 MW; 5031464104AF3DF6 CRC64;
MSLQKLENYS NKAVVQEEVL ILTELLEDIT KNMLAPETFA KIMELKELST QEDYQGLNQL
VTSLSNDEMA YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS ATIKMVAEKE
NAVEILEHLN VVPVLTAHPT QVQRKSMLDL TNHIHTLLRK YRDVKLGLIN KEKWHNDLRR
YIEIIMQTDM IREKKLKVTN EITNVMEYYN SSFLKAVPHL TAEYKRLAKK HGLELKHPKP
ITMGMWIGGD RDGNPFVTAD TLKQSAMTQC EVIMNYYDEK IYQLYREFSL STSIVNVSKQ
VREMARQSKD NSIYREKELY RRALFDIQSK IQATKAYLIE DKEVGARYET ANDFYKDLIT
IRDSLLENKG EALISGDFVE LIQAVEIFGF YLASIDMRQD SSVHEACVAE LLKSAGIHSH
YSELSEEEKC QLLLKELEED PRILSATHVE KSELLEKELA IFKAARKLKD KLGDDVIRQT
IISHATSVSD MLELAILLKE VGLVDKERAR VQIVPLFETI EDLDHSEETM REYLSLPLAK
KWIASRNNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKV TFFHGRGGTV
GRGGGPTYEA ITSQPLKSIK DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SAAINRMITQ
KKSDTNTSNR YEAIMDQVVD RSYDIYRDLV FGNDHFYDYF FESSPIKAIS SFNIGSRPAA
RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI DKNPENIAIL RDMYQNWPFF
QSLLSNVDMV LSKSNMNIAF EYAKLCEDEE VKAIYETILN EWQVTKEVIL AIEGYDELLA
ENPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE KLIHTTINGI ATGLRNSG
//
