ARCC1_ENTFC
ID ARCC1_ENTFC Reviewed; 310 AA.
AC P0A2X8; O54531; P35836;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Carbamate kinase 1;
DE EC=2.7.2.2;
GN Name=arcC1; Synonyms=arcC, arcC-1;
OS Enterococcus faecium (Streptococcus faecium).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=D10;
RX PubMed=9578487; DOI=10.1046/j.1432-1327.1998.2530280.x;
RA Marina A., Uriarte M., Barcelona B., Fresquet V., Cervera J., Rubio V.;
RT "Carbamate kinase from Enterococcus faecalis and Enterococcus faecium:
RT cloning of the genes, studies on the enzyme expressed in Escherichia coli,
RT and sequence similarity with N-acetyl-L-glutamate kinase.";
RL Eur. J. Biochem. 253:280-291(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-33 AND 159-169, AND CHARACTERIZATION.
RC STRAIN=D10;
RX PubMed=8308897; DOI=10.1006/jmbi.1994.1088;
RA Marina A., Bravo J., Fita I., Rubio V.;
RT "Crystallization, characterization and preliminary crystallographic studies
RT of carbamate kinase of Streptococcus faecium.";
RL J. Mol. Biol. 235:1345-1347(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF GLU-136; GLU-138;
RP LYS-140; GLU-141; ASP-208 AND ASP-210.
RC STRAIN=D10;
RX PubMed=10211841; DOI=10.1110/ps.8.4.934;
RA Marina A., Alzari P.M., Bravo J., Uriarte M., Barcelona B., Fita I.,
RA Rubio V.;
RT "Carbamate kinase: new structural machinery for making carbamoyl phosphate,
RT the common precursor of pyrimidines and arginine.";
RL Protein Sci. 8:934-940(1999).
CC -!- FUNCTION: Catalyzes the reversible synthesis of carbamate and ATP from
CC carbamoyl phosphate and ADP. Can also catalyze, although with low
CC efficiency, the phosphorylation of bicarbonate, leading to the
CC formation of carboxyphosphate, an unstable intermediate found in the
CC reactions catalyzed by carbamoyl-phosphate synthase and biotin
CC carboxylase. Can also use acetate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate +
CC H(+) + H2O; Xref=Rhea:RHEA:10152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=2.7.2.2;
CC -!- ACTIVITY REGULATION: Inhibited by
CC adenosine(5')pentaphospho(5')adenosine (Ap5A), Ap6A and to a much lower
CC extent by Ap4A.
CC -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate
CC degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer (predominantly) and homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By arginine.
CC -!- MASS SPECTROMETRY: Mass=32803; Mass_error=10; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9578487};
CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR EMBL; AJ223331; CAA11270.1; -; Genomic_DNA.
DR PIR; S44002; S44002.
DR PDB; 1B7B; X-ray; 2.80 A; A/B/C/D=1-310.
DR PDBsum; 1B7B; -.
DR AlphaFoldDB; P0A2X8; -.
DR SMR; P0A2X8; -.
DR UniPathway; UPA00996; UER00366.
DR EvolutionaryTrace; P0A2X8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008804; F:carbamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035975; P:carbamoyl phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04235; AAK_CK; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR003964; Carb_kinase.
DR PANTHER; PTHR30409; PTHR30409; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000723; Carbamate_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00746; arcC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8308897"
FT CHAIN 2..310
FT /note="Carbamate kinase 1"
FT /id="PRO_0000185124"
FT MUTAGEN 136
FT /note="E->A: No change in activity; when associated with A-
FT 138; A-140 and A-141."
FT /evidence="ECO:0000269|PubMed:10211841"
FT MUTAGEN 138
FT /note="E->A: No change in activity; when associated with A-
FT 136; A-140 and A-141."
FT /evidence="ECO:0000269|PubMed:10211841"
FT MUTAGEN 140
FT /note="K->A: No change in activity; when associated with A-
FT 136; A-138 and A-141."
FT /evidence="ECO:0000269|PubMed:10211841"
FT MUTAGEN 141
FT /note="E->A: No change in activity; when associated with A-
FT 136; A-138 and A-140."
FT /evidence="ECO:0000269|PubMed:10211841"
FT MUTAGEN 208
FT /note="D->A: Almost no activity; when associated with A-
FT 210."
FT /evidence="ECO:0000269|PubMed:10211841"
FT MUTAGEN 210
FT /note="D->A: Almost no activity; when associated with A-
FT 208."
FT /evidence="ECO:0000269|PubMed:10211841"
FT CONFLICT 169
FT /note="I -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1B7B"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1B7B"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1B7B"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1B7B"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1B7B"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1B7B"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1B7B"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1B7B"
SQ SEQUENCE 310 AA; 32927 MW; E214B3BA542A89D6 CRC64;
MGKKMVVALG GNAILSNDAS AHAQQQALVQ TSAYLVHLIK QGHRLIVSHG NGPQVGNLLL
QQQAADSEKN PAMPLDTCVA MTQGSIGYWL SNALNQELNK AGIKKQVATV LTQVVVDPAD
EAFKNPTKPI GPFLTEAEAK EAMQAGAIFK EDAGRGWRKV VPSPKPIDIH EAETINTLIK
NDIITISCGG GGIPVVGQEL KGVEAVIDKD FASEKLAELV DADALVILTG VDYVCINYGK
PDEKQLTNVT VAELEEYKQA GHFAPGSMLP KIEAAIQFVE SQPNKQAIIT SLENLGSMSG
DEIVGTVVTK
