ID D5C581_NITHN Unreviewed; 962 AA.
AC D5C581;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Nhal_2213 {ECO:0000313|EMBL:ADE15304.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15304.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001798; ADE15304.1; -; Genomic_DNA.
DR AlphaFoldDB; D5C581; -.
DR STRING; 472759.Nhal_2213; -.
DR KEGG; nhl:Nhal_2213; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000001844; 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:SF46; 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 Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 619
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 962 AA; 109063 MW; D2E4C47AA3F2DC3C CRC64;
MTPMMKQIPE AKPAPIASVS PDQTKNATPW RDKELRARVK LFGNLLGQVI QAQSREKVFA
AVEALRKGYI NLRKKENPDK RIQLLRLISK LDVETLTQVV RAFSIYFSLA NIAEEAYQHR
QRQRRIDAGG PLWRGSFEET LQEVRNGGVG PGQLQILLDS LAYIPVITAH PTEAKRRTVM
EHLRKIFLTS KLLDEARLSQ REEEALHRQL ERQIQVLWKT DEVRAHRPQV RDEIINGLFY
FKVSLFQAVP ETYRQLEEAI HKVYGDDLPE NTTIRVPSFL HFGSWIGGDR DGNPNVKPEI
TAMAVRLQMR MALRHYLERI GELMRILTHS IPLIQPSTAL MDSINQDLND CPEALLGNPT
RFSHEPYRRK LYLMRYRLLD NLRAVELHLK PESGLSPPSG VGYPSEDEFL QDLYLIRDSL
INHGDGNIAA GELQDLIRLV ESFGFYLLKL DIRQESSCHT EAVAELVKQA GLHPAYLDLS
ETERQQLLSE QLAREEGVPI DREQLTPPTR ETLEIFDVMA QMRREVSPRV FGTYVISMTH
AASHVLEVMF LGHLAGLAKH QQGQWHCDLQ ISPLFETIED LEHIEPVMTA LLDDPSYQAL
LQASGNQQEV MIGYSDSCKD GGILASSWKL YEAQKKVTAL TGDRGVDCRI FHGRGGTIGR
GGGPTFDAIL SQPRGTVHGQ IKFTEQGEVL SSRYSNTETA IYELDMGISG LIKASACLVQ
PPQEEKRDYL GVMDFLAEAG ERAYRELTEE TPGFQDYFYE ATPVNEIGLL NIGSRPSHRK
KGDRSKASVR AIAWVFGWAQ ARHTFPAWYG IGSALEQWRA GAPDRLAKLQ AMYQEWPYFR
AMLSNIQMSL AKAELRIAQQ YAELCLDPET GERIFAMLSA EYQRTVTQVL HIVGAHTLLE
ENPSLALSLR RRDPYLDPLN HIQLTLIQRT RDPLLTPVER QAWIDPLLRS INAIAAGMRN
TG
//
