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Database: UniProt/TrEMBL
Entry: A0A1W6SM08_9PROT
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ID   A0A1W6SM08_9PROT        Unreviewed;       937 AA.
AC   A0A1W6SM08;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=EBAPG3_002960 {ECO:0000313|EMBL:ARO86812.1};
OS   Nitrosospira lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86812.1, ECO:0000313|Proteomes:UP000012179};
RN   [1] {ECO:0000313|EMBL:ARO86812.1, ECO:0000313|Proteomes:UP000012179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APG3 {ECO:0000313|EMBL:ARO86812.1,
RC   ECO:0000313|Proteomes:UP000012179};
RX   PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA   Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA   Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT   "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT   bacterium from sandy lake sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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; CP021106; ARO86812.1; -; Genomic_DNA.
DR   RefSeq; WP_004175816.1; NZ_CP021106.3.
DR   AlphaFoldDB; A0A1W6SM08; -.
DR   KEGG; nlc:EBAPG3_002960; -.
DR   eggNOG; COG2352; Bacteria.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000012179; 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:ARO86812.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012179}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   937 AA;  105917 MW;  284984772A45F535 CRC64;
     MNSFATQNGG IDTNHTDEKD RPVKDDPLRE DIRLLGRMLG DTLREQEGEP TFDLVENIRQ
     TAIRFRREQD PKARQELDMI LNQLSNKATV AVVRAFSHFS QLSNIAEDMH HNRRRRTHLR
     AGSPPQAGSV ALALDRVFSS GTDGAALTGF FAKALVSPVL TAHPTEVQRR SILDCQLTIA
     HLLNERDRIQ LTPDELRSNE EGLRSAIQIL WQTRMLRPER LSVYDEIKNG LAYYRYTFLT
     EVPRLYAEIE DLLERRMGAD APHIPPFLRI GSWIGSDRDG NPFVTHEVML HAAERQSALA
     LDYYMGEVHL IGRRLSLTER LVGVDDELAA LSETSPDRAP SRIDEPYRRA LIGIYARLAA
     TSQELGHVIR QRRPVGPAAP YAEGTDFVHD LEIVIHSLKQ HKSDLLARGD LRHLRRAAEV
     FGFHLAPLDM RQHSNVHEQV VAELFEYGAH QRGYSELTEA ERIRWLLSEI TSPRPLRSPY
     LDYSELIQSE LCILQAAAEI QRRFGRAALP NYIISKTDGI SDILEVALLL KEVGLLQAGE
     IPHLHVNIIP LFETIADLRE CSRVMDDLFS LPYYRKLLDS RGNVQEVMLG YSDSNKDGGF
     LTANWELYKA ETELTKVFAK HKVELRLFHG RGGTVGRGGG PSYQAILAQP PGSVNGQIRI
     TEQGEVIGSK YADPEIGRRN LETLVAATVE ATLLSHDPLG ERAAEYYLIM EVLARDAFAA
     YRNLVYETPG FKRYFQESTP IREIAGLNIG SRPPSRKQSD LIEDLRAIPW VFSWSVNRAM
     IPGWYGFGTA VEAFVRREGQ GEKGLELLQE MHRTWPFMQT LLSNMDMVLA KTDMGIASRY
     AELVSDIGLR EEIFGRIQAE WDRSVKWLFA VTGRTELLQD NPTLARSIRN RTPYIDPLNH
     LQVELLRRYR SGDAADTVKR AIQLTINGVA AGLRNSG
//
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