ID F8GFD3_NITSI Unreviewed; 931 AA.
AC F8GFD3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 OrderedLocusNames=Nit79A3_0126 {ECO:0000313|EMBL:AEJ00033.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ00033.1};
RN [1] {ECO:0000313|EMBL:AEJ00033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ00033.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) 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 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; CP002876; AEJ00033.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GFD3; -.
DR STRING; 261292.Nit79A3_0126; -.
DR KEGG; nii:Nit79A3_0126; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 9768133at2; -.
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:AEJ00033.1}.
FT ACT_SITE 158
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 590
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 931 AA; 105735 MW; A5126BC008B0C341 CRC64;
MNAADSENNV ANNKLVDDKD LPLREDIRFL GRMLGDTLRE QDGDGAFELV ENIRQTAIRF
HRDQDLKARD ELDALLNRLS DKDSLPVVRA FSYFSLLSNI AEDVHHNRRR RAHLRAGSPP
QAGSVTLALE RVLESRKDIT VLAEFFNKAM ISPVLTAHPT EVQRRSILDC QLTIERLLKE
RARTELTPNE LRHNEEGLRA TIQILWQTRM LRPTRLSVYD EIENGLAYYS YTFLTEIPYI
YAKIEDLLER RLVKDVPYVT SFLRIGSWIG GDRDGNPFVT HDVMLRAVER QSSVALDFYI
DAVQKIGRSM SLTEQLVQVS DEVKQLAATA PDIPNRSDEP YRRIFLSIAA RLVATAHQLG
HQVTQYTPGE ARAPYASSTE FLHDLNAIIH SLKQHKSSWI ARGSLRNLCR AVDVFGFHLA
PLDMRQHSKI HEQVVGELFE HSTGRKGYAQ LSEKDRIEWL LKEISLPRSI LASYADFSEL
AQSELRILQC AAEIHRRFGR VAMSNYIISM TTDIINVLEV AFLLQQVGLL QAGENPQLFL
NIIPLFETIS DLRSCSNIMD QLFSLPYYRK LLSSRGNVQE VMLGYSDSNK DGGFITSNWE
IYKAEIELTK VFAKHQVELR LFHGRGGTVG RGGGPSYQSI LAQPPGSVNG QIRVTEQGEV
ISSKYAEPEI GRRNLETLVA ATLEATLLSH DSLGANADRY YPAMEMLASA SFAAYRDLVY
ETPGFKQFFL ESTPIREMAG LHIGSRPPSR KNSDAIEDLR AIPWVFSWSL SRMMLPGWYG
FGHAVEAFVN REDQPGQGLQ LLQEMYQNWP FMQTLLSNMD MVLTKTDMGI ASRYAELVED
VALREQIFGR IKDEWARSQK WLFAVTGHTE LLQDNPTLAR SIRNRTPYID PLNHLQVELL
RRYRSGEDSE EVKRSIHLTI NGVTAGLRNS G
//