ID A0A0C9M3N0_SPHPI Unreviewed; 891 AA.
AC A0A0C9M3N0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ECO:0000313|EMBL:GAN14490.1};
GN ORFNames=SP6_42_00480 {ECO:0000313|EMBL:GAN14490.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14490.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN14490.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14490.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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:GAN14490.1}.
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DR EMBL; BBJS01000042; GAN14490.1; -; Genomic_DNA.
DR RefSeq; WP_007405596.1; NZ_BBJS01000042.1.
DR AlphaFoldDB; A0A0C9M3N0; -.
DR GeneID; 78527783; -.
DR Proteomes; UP000032025; 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}.
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 558
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 891 AA; 96840 MW; 6960630634B3B789 CRC64;
MTTLPPIANN ADIRFLGAQL GDVIRRYGGD ALFEATEAIR RASVDRHRGL GDDAAVDLQL
ERLALDETLD FVRGFMLFSM LANLAEDRQG IAREPAADIA DVLETLAEQG IDRDTAMALL
GQALVVPVLT AHPTEVRRKS MIDHRNRIAE LLAMRDAGRD VTPDGDDVEA AIGRQIALLW
QTRVLRRERL YVTDEVETAL SYLRDVFLPV VPALYQRWDK AFGARVPAFL RPGSWIGGDR
DGNPFVTADS LTTALAQAAE AVLGHYCEAV HALGAELSIS TGHAEVDEAV LALAEASGDD
AVSRSDEPYR RALSGIYARL AATHEALTGK PAPRPGRLTG EPYPDPKALR TDLVAIARGL
AARGDGALAS GGALGRLIRA VETFGFHLAT LDLRQNSAVH ERVVAELLKV AGVEEDYLTL
DEEARVALLR RELANARPLV SRYADYSDET RSELAIVQAA AEAHARYGPK CITNYIVSMG
KSVSDLLEIN LMLKEFGLYR PGEPATAAIM AVPLFETIED LEAGPEIMRA YFGLPEIAAI
VRARGHQEVM IGYSDSNKDG GYLTSTWSLS KASSAFRPVF DEAGVRMQLF HGRGGAVGRG
GGSAFAAIRA QPHGTVQGRI RITEQGEVIA GKYGTRDSAM TNLEAMASAT LLASLEPERL
SADQNARFTG AMEQLSATAF RTYRDLVYGT EGFRTFFRQM TPIAEIAGLK IGSRPASRKK
SDAIEDLRAI PWVFSWAQAR VMLPGWFGVG TAIANFEDKA LLADMAKNWP FFAATLANME
MVLAKSDIGI AKRYAGLVED EGLRDTIFGR IHDGWHRARD GLLTVTGQPR LLSDNPALEA
SIRLRLPYIE PLNLLQIELM KRHRAGESDP RIGEGILLSI NGIATALRNS G
//
