ID A0A1I6TKN6_9BACI Unreviewed; 917 AA.
AC A0A1I6TKN6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05421668_1161 {ECO:0000313|EMBL:SFS89735.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS89735.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS89735.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS89735.1,
RC ECO:0000313|Proteomes:UP000199139};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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 ---------------------------------------------------------------------------
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; FPAI01000016; SFS89735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6TKN6; -.
DR STRING; 306541.SAMN05421668_1161; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000199139; 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; 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.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595}; Coiled coil {ECO:0000256|SAM:Coils};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:SFS89735.1}.
FT COILED 284..311
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 148
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 573
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 917 AA; 105382 MW; D0014BC6285D7A6D CRC64;
MHQQKTNGNT TLNQDVVYLN DILDTVLFNE GGEELLETVK YFRKLSKALR DEASPSNFDQ
LNQEIMKLAP ELRNKVIRAF SVNLQLYNIA EQNYRIRRRR EYQMEDDTII QPRSLEAGVN
ELYNHDITIE QVEKALEDLS LELVITAHPT EATRRTMLRI HQRIADLLKQ WEFSYTRYDK
KVIQEEIETE MTILWQTAEI REKKPSVMKE VSNGLYFFDK VLFNVLPVLH QDLEDLLYEK
YSHRFHVPAF LRFGSWIGGD RDGNPNVTAK ITYKTLKEQR ALVLTKYMES IDKLKEKLSQ
STKKVDVSED LLESIEKDKA ELNYRGWHKQ DEVYRVKLGM VMRRLRLTSE DQPGAYIDAH
ALREDLMLIQ DSLENHHSKS NPIKLLRHII RQVQLFGFHL ATLDVRNHSG EHEATITEIL
RQVGISEDYK ALSEGEKQHV LTKVLQDPRP LISIYDEFSE SSQEMIETFR TIKLAKDTFG
ERAIEVYLIS MAEAVSDVLE VLVLAKEVGL YRVYPDGHVK SRLHVAPLLE TIDDLKNGPT
IIKSLFDIPL YRKHIEARGD SQEIMLGYSD GSKDGGNLTA NWELYKAQED IHSVASSYGV
KLKFFHGRGG SLGRGGGPLY SSLLSQPPIT LGDGVKITEQ GEVLSSRYLI PDIAYRSLEQ
ATSVLLSSIA GIRQTEKHRE MPSDEAKDAM AFISEVSLKK YQDLVFNDDQ FLSYFNQGTP
LNELGALNIG SRPMKRKGSN RFEDLRAIPW VFAWTQSRQL IPAWYAAGTG LKAYLDETGN
IQLLREMYQQ WPFFRATINN LQMALTKADL EIADAYTDMI DDQEMAVRIF NDIRDEHKIT
KDMVLQIAQQ DDLMDHQPNI KESVRLRNPL VDPLNLIQVQ LVSRLRQVQE DSEEFNELLG
EVLLTINGIA AGLRNTG
//
