ID I4VVC9_9GAMM Unreviewed; 901 AA.
AC I4VVC9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=UU7_13998 {ECO:0000313|EMBL:EIL91170.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL91170.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL91170.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL91170.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL91170.1}.
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DR EMBL; AJXT01000045; EIL91170.1; -; Genomic_DNA.
DR RefSeq; WP_007809348.1; NZ_AJXT01000045.1.
DR AlphaFoldDB; I4VVC9; -.
DR STRING; 1163407.UU7_13998; -.
DR PATRIC; fig|1163407.3.peg.2818; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000003226; 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:EIL91170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226}.
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 568
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 901 AA; 100031 MW; 863F825B886ABFEF CRC64;
MEQSREPEFL PPDGPLREDV SRLGAMVGRM LAEQRGDAFF RRVEQVRTAA IHRRREGASV
DELADSLAGQ DAAQAEALAR AFATYFQAVN TAERVHRIRR RRDYQREGSA PQPESLLAVL
GRLKAEGVGA DELVGWLDRL WIEPVFTAHP TEAVRRSLLE KEQAIVASLI DGFDPQRTPQ
ECREDDQRIY MALSAGWQTA EASPVRPSVQ DEREHVDFYL THPLYRIVPA LYESLAQALQ
DTYGLAIRLP RLLRFASWVG GDMDGNPNVG ADTIADCLDS QRAMVIERYR EDVAALARAL
SQTEGRVEVT GALLARLADY RARFPAAAAQ IRPRHADMPY RCLLQLIGAR LALTQELQTD
GYASSQELLD DLQLIADSLL QHHGVHAGAY SVERLLCRVR TFGFHLARLD VRQDSRVHDD
ALAALLGDAE WASREGAERA DRLRPYASGE ARFPDSDDDS ATSLQAVFAT LRDSRQSHGV
EATGLYIISM ARSAADVLAV LALARRGGLV DETKDVPLNI APLFETVDDL RNAPATLRAL
LDDPVYRRHL AARGDQQWVM LGYSDSGKDG GTLASRWGLQ RAQVELLEVA NEARIQLAFF
HGRGGSASRG GARITPALMS SPRGAVAGVL RVTEQGEVIH RKYGIRALAL RNLEQTVGAV
LRASLRPRES EPRERRWREQ MDALSAASRK TYRAFVERAG FVDYFRSATP VDVIEQMTLG
SRPASRRSMR GVQDLRAIPW VFAWTQCRSI LPGWYGLGSA LEQGAGEFGE DALAGMARDW
PFFANLLDDV EMVLAKCDLD IAEAFSKLSG PLHDEFFGLI RDEFARTRHW LLQLKRSDAL
LQDAPRLAAS IRLRNPYVDP MSLLQVDLLQ RWRDGGRTDD AVLQALVACV NGVSQGLQNT
G
//
