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Database: UniProt/TrEMBL
Entry: F9ZCV7_9PROT
LinkDB: F9ZCV7_9PROT
Original site: F9ZCV7_9PROT 
ID   F9ZCV7_9PROT            Unreviewed;       933 AA.
AC   F9ZCV7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=NAL212_0449 {ECO:0000313|EMBL:ADZ25394.1};
OS   Nitrosomonas sp. AL212.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25394.1, ECO:0000313|Proteomes:UP000001629};
RN   [1] {ECO:0000313|EMBL:ADZ25394.1, ECO:0000313|Proteomes:UP000001629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL212 {ECO:0000313|EMBL:ADZ25394.1,
RC   ECO:0000313|Proteomes:UP000001629};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA   Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT   "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL   Submitted (FEB-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; CP002552; ADZ25394.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9ZCV7; -.
DR   STRING; 153948.NAL212_0449; -.
DR   KEGG; nit:NAL212_0449; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000001629; 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:ADZ25394.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001629}.
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   933 AA;  106088 MW;  524A51A41DB9EA05 CRC64;
     MNDVDSENYD TNANKLANDK DLPLREDIRF LGRMLGDTVR EQEGDKAFEL VENIRKIAIR
     FHREQDPAAR HELEAILKQL SDKDSLPVVR AFSYFSLLSN IAEDVHHNRR RRAHLRAGST
     PQAGSVTLAL ERVLESSSNA RTILADFFKQ AIVSPVLTAH PTEVQRRSIL DCQLAIERLL
     KERAWVELTP NEMRHNEENQ RATIQILWQT RMLRPTRLSV YDEIENGLAY YSYTFLSEIP
     YIYAKIEDLL ERRLAGDIPL VTSFLRIGSW IGGDRDGNPF VTHEVMLRAM ERQSAVALEY
     YMDAVQKIGR SMSLTERLVE VSDEVKKLLA TAPDIPNRSD EPYRRIFLSI GARLVATAKK
     FGHQVLQLST EETREPYAVS AEFVHDLEAI IQSLKQHKSS WVARGALRNL RRAADVFGFH
     LAPLDMRQHS KIHEQVVSEL FEYYTGHKDY LQLSEEERID WLLSEINRLH PLLTIPSEFS
     ETTQSELRIL QCAAEIHRRF GRAAMPNYII SMTTGVINIL EVAYLLRQVD LLQTGENPQL
     HLNIIPLFET ISDLQSCGKI MDQLFSLPYY RKLLSSMGSV QEVMLGYSDS NKDGGFIASN
     WEIYKAEIAL TKVFAKHQIG LRLFHGRGGT VGRGGGPSYQ SILAQPPGSV NGQIRVTEQG
     EVISSKYAEP EIGRRNLETL VAATMEATLL GHDSIGSNAD QYYPAMNKLA AISFAAYQDL
     VFGTTGFKQF FLESTPIREM AGLHIGSRPP SRTSSDDIED LRAIPWVFSW SQSRMMLPGW
     YGFGHAVETF VTQKDQNGQG LALLQEMYQK WPFMQTLLSN MDMVLAKTDM GIASRYAELV
     NDIALREQIF ARIREERARS EKWLFAITGN VELLQDNPTL ARSIRNRIPY IDPLNHLQVE
     LLRRYRSGED SEEVKRSIHL TINGVTAGLR NSG
//
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