ID   F4H3H5_CELFA            Unreviewed;       897 AA.
AC   F4H3H5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=Celf_2393 {ECO:0000313|EMBL:AEE46520.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE46520.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE46520.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-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; Evidence={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}.
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DR   EMBL; CP002666; AEE46520.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4H3H5; -.
DR   STRING; 590998.Celf_2393; -.
DR   KEGG; cfi:Celf_2393; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000008460; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:AEE46520.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        564
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   897 AA;  98974 MW;  AC9580C5D834B07B CRC64;
     MAYFGPVTAP LPPRDVRRGL ARHEVPEPLR NDVRVLGEFL GRVLRESVGQ DLLDDVEQLR
     ELAIRAHDEQ DGDALEQAEA LVAGFSLERA EQVARAFTCY FHLANTAEEY HRIRVLRERE
     ASLQPHDLAP DDSLPAAVER AREELGTDVA LQRVQELEFR PVFTAHPTEA RRRAVSNAIR
     RIAELVGERD IRSRGGMSIA ENDRRLLAEI DTLWRTAPLR QEKPTVLDEV RTVLNVFDST
     LSDVLPAVYR RLDDWLLGDD AGTRAPAVRP FARLGTWIGG DRDGNPNVTA EVTRAAALLA
     SEHALKALET TARRTANGLT LGSDTTPPSQ ELSALWQRQR GIAEQLAAQA ASDAPNEPHR
     RVLQVVTERI AATRRRDADL AYATPDELEA DLLVVQRSLV EAGATRSAYG DLQRLLWQVR
     TFGFHLAELE VRQHSQVHEA ALADIAEHGV DGELQPRTLE VLDTFRALGA VQRRFGQDAA
     RRYIVSFTQS AQHLAAVYQL AELAYGGPDE VPVIDAVPLF ETFADLEASV DILEEALTLP
     QVQRRLADNG RRVEVMLGYS DSSKDVGPVS ATLALDAAQR RITEWAREHD IQLTLFHGRG
     GALGRGGGPA NRAVLAQPPG SVDGRFKLTE QGEVIFARYG DPVIAARHIE QVVAATLLAG
     TPSVERRNAA ATERFAGLAR QLDEASRTRF HELVRADGFP QWFAQVTPLE EVGLLPIGSR
     PARRGLSVSS LDDLRAIPWV FSWSQARINL AGWYGLGSAL DAVGDLDELR DAYAQWPLFT
     TMIDNVEMSL AKTDERIAAR YLALGDRPDL AERVLTEMSL TRRSVLAITD SDAVLSRRRI
     LGRAVQLRSP YVDALSLLQL RALRGLRTGD APERADDLRR LLLLTVNGVA AGVQNTG
//