ID A0A1V2ESM6_9SPHN Unreviewed; 889 AA.
AC A0A1V2ESM6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:ONF95676.1};
GN ORFNames=SPHI_21130 {ECO:0000313|EMBL:ONF95676.1};
OS Sphingomonas jeddahensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1915074 {ECO:0000313|EMBL:ONF95676.1, ECO:0000313|Proteomes:UP000188729};
RN [1] {ECO:0000313|EMBL:ONF95676.1, ECO:0000313|Proteomes:UP000188729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G39 {ECO:0000313|EMBL:ONF95676.1,
RC ECO:0000313|Proteomes:UP000188729};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas jeddahensis G39.";
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}.
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:ONF95676.1}.
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DR EMBL; MPSB01000009; ONF95676.1; -; Genomic_DNA.
DR RefSeq; WP_076744881.1; NZ_MPSB01000009.1.
DR AlphaFoldDB; A0A1V2ESM6; -.
DR STRING; 1915074.SPHI_21130; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000188729; 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:ONF95676.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188729}.
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 556
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 889 AA; 95960 MW; 898750C743BEF7FD CRC64;
MSTLPPITNN DDIRYLGRVL GDVIREMGGT RLFAATEAIR SASVERHRDG GAPVDHHLEA
LSLDETLDFV RGFMLFSMLA NLAEDRHGIA AEEGADVASA LERLAGEGID QDAVCALLEH
ALIAPVLTAH PTEVRRKSMI DHRNRIAELM AMRDMGAEET PDGDRIDEAI VRQVALLWQT
RVLRRERLYV TDEVETALSY LRDVFLPVIP ALYQRWDRAM GRRLPAFLRP GSWIGGDRDG
NPFVTADSLR AALAKAAAAA IGYYLDQLHA LGSELSISAD HAPVDAAVLA LAEASGDNAE
SRIDEPYRRA LSGIYARLAA TYEALVGTQP PRPGARRAEP YPDPHALRAD LVALAKPLAA
AAGGLLASGG AIGRLIRAVE VFGFHLATLD LRQNSAVHER VVAELLKTAG VCEDYLGLDE
DERVALLNRE LASARPLTSR YIDYSQETAG ELAIVAAVAE AHAAYGPACI RQYIVSMCQS
VSDLLEVHLL LKEVGLYVPG DPPQAAVMAV PLFETIGDLE AAPGIMQAWF ALPEVAAIAT
ARGHQEVMIG YSDSNKDGGY LTSGWQLSKA STALKPVFEA AGVGMQLFHG RGGAVGRGGG
SAFAAIRAQP PGTVQGRIRI TEQGEVIAGK YGTRESAITN LEAMTSATLL TSLSPAPLSN
AENESFAKAM DRLSDTAFHA YRDLVYGTEG FNAFFRQMTP IAEISGLKIG SRPASRKKSA
KIEDLRAIPW VFSWAQARVM LPGWYGVGHA IAAFEDKALL AEMAEGWPLF AATLANMEMV
LAKSDMGIAE RYAGLVEDDK LGARIFGRIK DDWQATCDGL LEVTGQSRLL DKHPALDASI
RLRLPYIEPL NLLQIELMRR HRAGEDDPRI AEGILLSINA IATALRNSG
//
