ID F4H3H5_CELFA Unreviewed; 897 AA.
AC F4H3H5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 28-MAR-2018, entry version 47.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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; Actinobacteria; 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.,
RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA Mead D., Brumm P., 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
CC source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC ECO:0000256|SAAS:SAAS00946751}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR EMBL; CP002666; AEE46520.1; -; Genomic_DNA.
DR RefSeq; WP_013771546.1; NC_015514.1.
DR STRING; 590998.Celf_2393; -.
DR EnsemblBacteria; AEE46520; AEE46520; Celf_2393.
DR KEGG; cfi:Celf_2393; -.
DR eggNOG; ENOG4105CCA; Bacteria.
DR eggNOG; COG2352; LUCA.
DR KO; K01595; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; POG091H040O; -.
DR BioCyc; CFIM590998:G1GXC-2414-MONOMER; -.
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 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; PTHR30523; 2.
DR Pfam; PF00311; PEPcase; 2.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW ECO:0000256|SAAS:SAAS00946757};
KW Complete proteome {ECO:0000313|Proteomes:UP000008460};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW ECO:0000313|EMBL:AEE46520.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW ECO:0000256|SAAS:SAAS00946750};
KW Pyruvate {ECO:0000313|EMBL:AEE46520.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT ACT_SITE 166 166 {ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111}.
FT ACT_SITE 564 564 {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
//
