ID Q5NME0_ZYMMO Unreviewed; 885 AA.
AC Q5NME0;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 123.
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=ZMO1496 {ECO:0000313|EMBL:AAV90120.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV90120.1, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV90120.1, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV90120.1; -; Genomic_DNA.
DR RefSeq; WP_011241269.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NME0; -.
DR SMR; Q5NME0; -.
DR STRING; 264203.ZMO1496; -.
DR KEGG; zmo:ZMO1496; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_5; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000001173; 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 Reference proteome {ECO:0000313|Proteomes:UP000001173}.
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 552
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 885 AA; 98750 MW; 77F9A32B225FDA7C CRC64;
MTKPRTINQN PDLRYFGNLL GQVIKEQGGE SLFNQIEQIR SAAIRRHRGI VDSTELSSRL
ADLDLNDMFS FAHAFLLFSM LANLADDRQG DALDPDANMA SALKDIKAKG VSQQAIIDMI
DKACIVPVLT AHPTEVRRKS MLDHYNRIAG LMRLKDAGQT VTEDGLPIED ALIQQITILW
QTRPLMLQKL TVADEIETAL SFLRETFLPV LPQIYAEWEK LLGSSIPSFI RPGNWIGGDR
DGNPNVNADT IMLSLKRSSE TVLTDYLNRL DKLLSNLSVS TDMVSVSDDI LRLADKSGDD
AAIRADEPYR RALNGIYDRL AATYRQIAGR NPSRPALRSA EAYKRPQELL ADLKTLAEGL
GKLAEGSFKA LIRSVETFGF HLATLDLRQN SQVHERVVNE LLRTATVEAD YLSLSEEDRV
KLLRRELSQP RTLFVPRADY SEETRSELDI IQAAARAHEI FGPESITTYL ISNGESISDI
LEVYLLLKEA GLYQGGAKPK AAIEAAPLFE TVADLENAPK VMEEWFKLPE AQAIAKAHGV
QEVMVGYSDS NKDGGYLTSV WGLYKACLAL VPIFEKAGVP IQFFHGRGGS VGRGGGSNFN
AILSQPAGAV KGRIRYTEQG EVVAAKYGTH ESAIAHLDEA VAATLITSLE APTIVEPEFS
RYRKALDQIS DSAFQAYRQL VYGTKGFRKF FSEFTPLPEI ALLKIGSRPP SRKKSDRIED
LRAIPWVFSW SQVRVMLPGW FGFGQALYDF EDTELLQEMA SRWPFFRTTI RNMEQVMARS
DMTIAKHYLA LVEDQTNGEA IYDSIADGWN KGCEGLLKAT QQNWLLERFP AVDNSVQMRR
PYLEPLNYLQ VELLKKWRGG DTNPHILESI QLTINAIATA LRNSG
//