ID A0A1M7EYU2_9GAMM Unreviewed; 882 AA.
AC A0A1M7EYU2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05878437_0523 {ECO:0000313|EMBL:SHL96599.1};
OS Halomonas subglaciescola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=29571 {ECO:0000313|EMBL:SHL96599.1, ECO:0000313|Proteomes:UP000190911};
RN [1] {ECO:0000313|EMBL:SHL96599.1, ECO:0000313|Proteomes:UP000190911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 12 {ECO:0000313|EMBL:SHL96599.1,
RC ECO:0000313|Proteomes:UP000190911};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|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; LT670847; SHL96599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7EYU2; -.
DR STRING; 29571.SAMN05878437_0523; -.
DR InParanoid; A0A1M7EYU2; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000190911; Chromosome i.
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:SHL96599.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190911}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 546
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 882 AA; 98797 MW; 7AAF3DA224512EF0 CRC64;
MSHDLHESLR DNVRILGDSL GHTIADDLGQ AFVDKIETIR SYAKQGRQKD TLEQRELIDY
LRKLPDNDLL PVTRAFNQFL NLANIAEQHY RARFRHVEDY KPGSQPTLEK LLERAQQAGS
SPRALVQTLA DMRVELVLTA HPTEIIRRTL IQKYDAIDDC LSAIEGAEDA PERATRARGR
LAELISQAWH TDEIRHERPT PVDEAKWGFA VIENSLWQAV PDFHRDLDNL LLDTAGERLP
LDAAPIRYAS WMGGDRDGNP NVTASVTREV LLLGRWMAAD LYLRDLEQLK NELSMWKANS
ALKAEVGDVA EPYRELLKRI VTRMQATRDW AKAGLDGRSF DGGPIIETRD QLYAPLLSCY
RSLCDSGLDV IANGALLDTL RRVAVFGVTL TKLDLRQEAS RHAQVLEEIT HELELGHYQD
WNEAERQAFL LTELKSNRPL IPLRWQCSAE TREVLETFRV VAEEQPEALG SYVISMAAEP
SDVLTVALLM QEVGGRAALP IAPLFETLND LDHAGEVIDQ LLALPEYRAL MQGRQEVMIG
YSDSAKDAGQ LAAAWAQYRA QEALVEVCRK HDVKLTLFHG RGGAVGRGGG PAHAAILSQP
PGSVDGSLRV TEQGEMIRFK FGQPDIALRS MEIYACAVLE ATLLPPPAPK ANWRDEMDQL
AEVSHEVYVN VVRDDPEFVP YFRAVTPESV LGRLPLGSRP TKRRQDGGVE TLRAIPWIFA
WTQTRLMLPA WLGSEQAFSG RLEQPGGREV LQEMRDQWPF FGTYLDMLEM LLAKADVGIA
AYYEQRLVDE PALKALGTKL RERFELLEGS VLTLLEQDDL LEKTPLIRQA IEVRNPYIDP
LHGLQAELLQ RNRDADGAIS ADLSRALMVT MAGISAGLRN TG
//