ID Q2Y5J3_NITMU Unreviewed; 937 AA. AC Q2Y5J3; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 119. 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=Nmul_A2691 {ECO:0000313|EMBL:ABB75978.1}; GN ORFNames=SAMN05216403_10977 {ECO:0000313|EMBL:SEF79197.1}; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB75978.1, ECO:0000313|Proteomes:UP000002718}; RN [1] {ECO:0000313|EMBL:ABB75978.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB75978.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71 RC {ECO:0000313|Proteomes:UP000002718}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ABB75978.1, ECO:0000313|Proteomes:UP000002718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB75978.1}, and ATCC 25196 / RC NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718}; RX PubMed=18390676; DOI=10.1128/AEM.02722-07; RA Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S., RA Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.; RT "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing RT bacterium from the soil environment."; RL Appl. Environ. Microbiol. 74:3559-3572(2008). RN [4] {ECO:0000313|EMBL:SEF79197.1, ECO:0000313|Proteomes:UP000236751} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nl13 {ECO:0000313|EMBL:SEF79197.1, RC ECO:0000313|Proteomes:UP000236751}; RA de Groot N.N.; RL Submitted (OCT-2016) 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, ECO:0000256|HAMAP- CC 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; CP000103; ABB75978.1; -; Genomic_DNA. DR EMBL; FNVK01000009; SEF79197.1; -; Genomic_DNA. DR RefSeq; WP_011381970.1; NZ_FNVK01000009.1. DR AlphaFoldDB; Q2Y5J3; -. DR STRING; 323848.Nmul_A2691; -. DR KEGG; nmu:Nmul_A2691; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_4; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000002718; Chromosome. DR Proteomes; UP000236751; Unassembled WGS sequence. 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:SEF79197.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002718}. FT REGION 1..26 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; 105629 MW; DF00A8445BE07BAB CRC64; MASLASPSES IDTNPNYIHD KEPKDDPLRE DIRLLGRMLG DTLREQEGEP TFDLVENIRQ TAIRFRRDQD PKARQELDRL LNQLSNKATE AVVRAFSQFS QLSNIAEDMH HNRRRRSYLL ARSQPQAGSV ARALDLVFSK ETSSAALGRF FDKALVSPVL TAHPTEVQRR SILDCQLAIA RLLNERDRVQ LTPDELSKNE EGLRTNIQIL WQTRMLRSAR LSVYDEIKNG LAYYHYTFLT EVPHLYAEIE DLLERRMGDK APRIPPFLRI GSWIGGDRDG NPFVTHEVLL HAAERQSALA LDFYMGEVHR IGRRLSLTDR LVDVDEALAA LAEASPDRAP SRADEPYRRA LIGIYARLAA TSMGLGHAIR QRRPVGPAEP YTDSLELVRD LDIVIHSLEQ HKSELLARGD LRRVRRAAEV FGFHLAPLDM RQHSHIHEQV VAELFERGAN LKGYSDLPEA ERVRCLLTEV SSPRLLRSPY LDYSELAQSE LHIVETAAEI HRRFGPAALP NYVISKADGI SDILEVALLL KEVGLLRAGE KPCLHINIVP LFETIADLRG CARIMDELFS IPYYRKLVDS RNDVQEVMLG YSDSNKDGGF LAANWELYKA ETELTKVFAK HKVELRLFHG RGGTVGRGGG PSYQAILAQP PGSVNGQIRI TEQGEVIGSK YSDPEIGRRN LETLVAATIE ATLLSHDTLG QCADEYYGVM EVLAGDALRA YRSLVYETPG FNRYFQESTP IKEIAGLNIG SRPPSRKKSD LIEDLRAIPW TFSWGVNRAM ITGWYGFGTA VEMFVQREGK GDNGLGLLQK MYQAWPFLQT LLSNMDMVLA KTDMGIASRY AELVTDVELR REVFGRIQKE WELSVKWLFA VTGRTELLQD NPTLARSIRN RTPYIDPLNH LQVELLRRYR SGDATDAVTR AIQLTINGVA AGLRNSG //