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
//