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Database: UniProt
Entry: W7WX22_9BURK
LinkDB: W7WX22_9BURK
Original site: W7WX22_9BURK 
ID   W7WX22_9BURK            Unreviewed;       920 AA.
AC   W7WX22;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   Name=ppc_1 {ECO:0000313|EMBL:EWS61020.1};
GN   ORFNames=Y694_01207 {ECO:0000313|EMBL:EWS61020.1};
OS   Methylibium sp. T29-B.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=1437443 {ECO:0000313|EMBL:EWS61020.1, ECO:0000313|Proteomes:UP000019360};
RN   [1] {ECO:0000313|EMBL:EWS61020.1, ECO:0000313|Proteomes:UP000019360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T29-B {ECO:0000313|EMBL:EWS61020.1,
RC   ECO:0000313|Proteomes:UP000019360};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of the loss-of-function mutant Methylibium sp. T29-B.";
RL   Submitted (DEC-2013) 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   -!- 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:EWS61020.1}.
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DR   EMBL; AZSN01000021; EWS61020.1; -; Genomic_DNA.
DR   RefSeq; WP_036230605.1; NZ_AZSN01000021.1.
DR   AlphaFoldDB; W7WX22; -.
DR   PATRIC; fig|1437443.4.peg.1211; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000019360; Unassembled WGS sequence.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF32; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EWS61020.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:EWS61020.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   920 AA;  102414 MW;  ADBF60DE98E3F5FE CRC64;
     MGERSRPDLA DPDESAAGAE RADALARSEL LRAALIGVIE RYEPEVARVL RGEAPQERMS
     TRLLARTIQA QAIWFQLLAI AEQNRDMRRR REVERQRGHA QVRGTFAHVF HTAVEAGLDA
     KQIREALCSL RIRPVITAHP TEAKRVTVLE RHRRIYLRLF DLESPRWTDR EREDLTRAIS
     DEVELLWLTG ELKLDKPTVD QEVAWGLYFF DENLFDVVPQ LYGRIEAAFA KQFPGETLEL
     PVVFGFGSWI GGDRDGNPFV TSTVTRHTLW QMRLASLRRY RSRLADLARN LSISERAAAL
     PEDFRAAVAA ALAALPDGAG VAARNPGELF RQFIAGMLAR LDATIARNGE QPEPADAARD
     AAPYEHADQL IGDIELMHRA LVETGAQPLA KTFLAPLLRE VRTFRFATVR LDIRENTIRI
     NATLGELYRA VRGSEPPASD SAEWKDWLLT ELAAPRRAGE APLATAGLTP EAQETLATFR
     TVAEMRDRVD REAFGTLILS MTHSATDVLG VYLLAKHAGL FNDAQAVERC TLPVVPLLET
     IPDLRRAPAI LKELLAVPLV QRSLRLHGNV QEVMIGYSDS NKDGGYFTAN WELSKAQATM
     TRLGEDLGVK IAFFHGRGGS VSRGGAPTGR AIAALPAGSI RGGFRSTEQG EVVSYKYANR
     GTAHYQVELL ASSVLQHVLL SERESALVPK HEFDEAMEAI SGVSWTAYRQ LMESEHLLAY
     LQGSSPLEEL ALLNIGSRPA RRTQARTLAD LRAIPWVFAW TQNRHMLTGW YGLGSGLAAF
     VEVRKARGLD LLQRMFHEGR LFRTVIDEVE KTLLTVDLDI AREFAGLVAD PAVREPIFQA
     IEREYRLTCE MVLKVSGGRQ VAERFPQLRR RLARRLQTMN QVSREQVQLL RALRDGGDDD
     VRTAFLLSIN CAAAGLGATG
//
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