ID A0A2A5YHS3_9SPHN Unreviewed; 900 AA.
AC A0A2A5YHS3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CNE89_13480 {ECO:0000313|EMBL:PDH64196.1};
OS Sphingomonadaceae bacterium MED-G03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae.
OX NCBI_TaxID=1986231 {ECO:0000313|EMBL:PDH64196.1, ECO:0000313|Proteomes:UP000219365};
RN [1] {ECO:0000313|EMBL:PDH64196.1, ECO:0000313|Proteomes:UP000219365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G03 {ECO:0000313|EMBL:PDH64196.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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:PDH64196.1}.
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DR EMBL; NTKY01000050; PDH64196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5YHS3; -.
DR Proteomes; UP000219365; 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:PDH64196.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 567
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 900 AA; 97544 MW; 403DB65ED2D89546 CRC64;
MATPAPTPSA PAITQNPDIR YLGRLLGDVI RAYGGEKLYQ QTEYIRSASV DRARGVQGAD
LTDTGLDALG LDDTLNFTRG FMLFSMLANL AEDRQGVAAE PGADVASAMK RLDSHGVGRD
AVLDLLAHSL IVPVLTAHPT EVRRKSMIDH KNRIADLMHL KDAGRTETAD GENLDEAIFR
QIALLWQTRP LRREKLFVAD EIENVLAYFR DSFLPVLPAL YARWERVLGA RPQSFLRVGS
WIGGDRDGNP FVQAPQLQYA LRRGAAAAIA YYLDGVHALG AELSLSTELA HVPQAVLDLA
EASGDDAPSR KDEPYRRALS GIYARLAATC VSLTGAQPAR PSSLKGEPYA SPAELRHDLV
VVAQGLASEG NGALASGGAL GRLIRAVETF GFHLATLDMR QNSAVHERVV AELLKVAGVE
GDYLALDEYA RIALLRRELA NNRPLGSRFS AYSEETASEL AIVHAAAEAH RLYGPQCITH
YIISMAQSVS DLLEVNILLK EAGLWRVGDN GDPPHAAIMA IPLFETIGDL EAAPKIMSAY
FGLPEIAGVV KARGHQEVMI GYSDSNKDGG YITSTWGLYK ASQALEPVFA QAGAAMQLFH
GRGGAVGRGG GSAFAAIQAQ PRGSVQGRIR ITEQGEVIAA KFGTRDVAMT NLEAMTSATL
LASLEPEAIS ERDATRFAGA MDELSKNAFA AYRDLVYGTE GFRDFFRQLT PIQEIAGLKI
GSRPASRKKS TRIEDLRAIP WVFSWAQARV MLPGWYGVGQ ALAGFEDKAL LADMAQHWAF
LKSALANMEM VLAKSDLGIA ARYLPLVEDQ DGAQAIFGRI REGWQAAHDG LLHCTGQSRL
LEKNPALETS IRLRLPYIEP LNLLQVELLK RHRAGEEDPR IKEGIELSIN AIATALRNSG
//
