ID F0KI55_ACICP Unreviewed; 894 AA. AC F0KI55; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 62. 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 ECO:0000313|EMBL:ADY83508.1}; GN OrderedLocusNames=BDGL_002922 {ECO:0000313|EMBL:ADY83508.1}; OS Acinetobacter calcoaceticus (strain PHEA-2). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83508.1, ECO:0000313|Proteomes:UP000007477}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHEA-2; RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.; RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into RT environmental adaptation."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADY83508.1, ECO:0000313|Proteomes:UP000007477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83508.1, RC ECO:0000313|Proteomes:UP000007477}; RX PubMed=21441526; DOI=10.1128/JB.00261-11; RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z., RA Yuan M., Zhou Z., Elmerich C., Lin M.; RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from RT industry wastewater."; RL J. Bacteriol. 193:2672-2673(2011). 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; CP002177; ADY83508.1; -; Genomic_DNA. DR RefSeq; WP_014208009.1; NC_016603.1. DR RefSeq; YP_004997190.1; NC_016603.1. DR AlphaFoldDB; F0KI55; -. DR STRING; 871585.BDGL_002922; -. DR GeneID; 11637569; -. DR KEGG; acc:BDGL_002922; -. DR PATRIC; fig|871585.3.peg.2921; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_6; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000007477; 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}; Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000007477}. FT COILED 806..833 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 143 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 556 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 894 AA; 102030 MW; 338DCF7DE8D507DB CRC64; MVQQIDAPLR EDVRLLGNLL GETLKQHAGQ ELFNQIEQIR ALAKGARDGQ AEAEKQLEQL FLELPDEELL PLTRAFSHFL NFANIAEQYH VVRSRRQAEF DSDANSPNPL VHLFQKFKDK SISTEKLFQQ ICDLKIELVL TAHPTEVSRR TLIQKYDDIN ACLSQLDQQK LTPRERQNAL ANLKQQISSA WQTDEIRQHR PTPVDEAKWG FATIEQTLWN AVPKFIRELN ELVQENCQLN LPLNIAPVRF ASWMGGDRDG NPNVTHQITQ EVLWLSRWQA ADLYLRDIEN LRWELSIQTC SEEMIQAIGS QHAEPYREYL RATRERLKAT RHWLAQRLQG LEADDSNVIK SKDELLQPLL LCYRSLIDSN LPEIANGQLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN FESWTEQARQ NFLIQELQSK RPLLPKYINE PEGSLIGHPD VQEVFATMRT LADQPPESLG AYIISMAEYP SDVLAVLLLQ KEAGIQHPLR VVPLFETLKD LDGAATTMNT LFNMHWYKQH IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAIAQT HGVQLTLFHG RGGSISRGGA PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIAMQN LEIYTAATLE ATLLPPPEPK AEWRELMNRM TDHSVKVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE SLRAIPWVFA WTQIRLMLPA WLGTGAAINE VIADQQKATL DEMLQQWPYF QTLIDMLEMV LSKADANIAL YYESHLTEDE DLKVLGNQLR QRLKDAVETL LKLKDESKLL SNNEVLDQSM QVRKPYLLPL HLLQAELMKR RRDYLAERQA EHTPVDHALM VSIAGIAAGL RNTG //