ARCC1_ENTFA
ID ARCC1_ENTFA Reviewed; 310 AA.
AC P0A2X7; O54531; P35836;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Carbamate kinase 1;
DE EC=2.7.2.2;
GN Name=arcC1; Synonyms=arcC, arcC-1; OrderedLocusNames=EF_0106;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 29212 / DSM 2570;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29212 / DSM 2570;
RX PubMed=12399499; DOI=10.1128/jb.184.22.6289-6300.2002;
RA Barcelona-Andres B., Marina A., Rubio V.;
RT "Gene structure, organization, expression, and potential regulatory
RT mechanisms of arginine catabolism in Enterococcus faecalis.";
RL J. Bacteriol. 184:6289-6300(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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 -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR EMBL; AJ223332; CAA11271.1; -; Genomic_DNA.
DR EMBL; AJ312276; CAC41343.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO79981.1; -; Genomic_DNA.
DR RefSeq; NP_813909.1; NC_004668.1.
DR RefSeq; WP_002356132.1; NZ_KE136524.1.
DR PDB; 2WE4; X-ray; 2.02 A; A/B/C/D=1-310.
DR PDB; 2WE5; X-ray; 1.39 A; A/B/C=1-310.
DR PDBsum; 2WE4; -.
DR PDBsum; 2WE5; -.
DR AlphaFoldDB; P0A2X7; -.
DR SMR; P0A2X7; -.
DR STRING; 226185.EF_0106; -.
DR EnsemblBacteria; AAO79981; AAO79981; EF_0106.
DR GeneID; 60892655; -.
DR KEGG; efa:EF0106; -.
DR PATRIC; fig|226185.45.peg.154; -.
DR eggNOG; COG0549; Bacteria.
DR HOGENOM; CLU_076278_0_0_9; -.
DR OMA; QPMDVAG; -.
DR BRENDA; 2.7.2.2; 2095.
DR SABIO-RK; P0A2X7; -.
DR UniPathway; UPA00996; UER00366.
DR EvolutionaryTrace; P0A2X7; -.
DR Proteomes; UP000001415; Chromosome.
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; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..310
FT /note="Carbamate kinase 1"
FT /id="PRO_0000185122"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2WE4"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2WE5"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2WE5"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2WE4"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2WE5"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2WE4"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2WE5"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2WE5"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:2WE5"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2WE5"
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
