ID B6IUK4_RHOCS Unreviewed; 902 AA.
AC B6IUK4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:ACI99829.1};
GN OrderedLocusNames=RC1_2446 {ECO:0000313|EMBL:ACI99829.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99829.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI99829.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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; CP000613; ACI99829.1; -; Genomic_DNA.
DR RefSeq; WP_012567611.1; NC_011420.2.
DR AlphaFoldDB; B6IUK4; -.
DR STRING; 414684.RC1_2446; -.
DR KEGG; rce:RC1_2446; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_5; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000001591; Chromosome.
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:ACI99829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 570
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 902 AA; 98883 MW; 3624D660BDF5F195 CRC64;
MLNESDGVGD WPARNDVRLL GRLLGDVIRQ HDGQELFDRI EAIRKASIAA HREPGVANDA
HLAAQLHALE LDDMLRFVRG FLWFSLLANL AEDRQARRDA TERHVPGRPD TLARAVEVLE
AKGVSRAAVA ELLDHALISP VLTAHPTEVR RKSVIDREAA IGQLMQALDA AADRETRDGI
LADLYREIAI LWNTRALREA RITVADEIDT ALSYFRATFL EVLPRLHARW EGVLGNGPLP
AFLRLGSWIG GDRDGNPNVS AATLTQALKQ QARRALGHYL EELHALGGQL SICADISPPS
AELEHLAEIS GDTSPHRADE PYRRALTGLY ARTAATYRQL VGEAPPRSPA VPGDPYPDAA
ALLADLRVVR DSLARGSAPI VDRRLNELIN AVDLFGFHLA TLDLRQNADV HGRVVAELLR
VAGVEDNYLG LPEPARVALL RRELAHLRLL CNPFAGYSDE TRRELEILRT LAASHERYGA
GCVRQYIVSK TSGVSNLLEV HLLLKEAGMF RPGDPPFGAV MAVPLFETIE DLAAAPLVMR
EYLGFPEIRA LALSCWGFQE VMLGYSDSNK DGGYLTSNWS LHEAACALRH VFDEAGVRLQ
LFHGRGGAVG RGGGSAFAAI RAQPSGTVGG RIRITEQGEV IAAKYGNTTV GTASLETMVA
AVVLASLEPG GLREDMSRFR LAMQGMSRSA FHAYRALVYD TPGFKDFFRA ATPIAEIADL
KIGSRPASRT TLDRIEDLRA IPWVFSWTQA RIMLPGWYGV GTALESFPDR GLLEAMYEGW
PFLQAALSNL EMVLAKTDMD VAATYAGLVP DEALRTRVFS AIRSEWQRTH DQLLALTGQS
ELLQHAPAVA RSIRLRLPYV EPLNLLQVEL IRRHRAGETA PEIRDGIHLT INGIATSLRN
SG
//
