ID   CBK_GIAIN               Reviewed;         317 AA.
AC   O97438;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Carbamate kinase;
DE            EC=2.7.2.2;
GN   Name=CBK;
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   CHARACTERIZATION.
RC   STRAIN=Portland-1;
RX   PubMed=10029308; DOI=10.1016/s0166-6851(98)00141-8;
RA   Minotto L., Tutticci E.A., Bagnara A.S., Schofield P.J., Edwards M.R.;
RT   "Characterisation and expression of the carbamate kinase gene from Giardia
RT   intestinalis.";
RL   Mol. Biochem. Parasitol. 98:43-51(1999).
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   -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate
CC       degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF017784; AAD13336.1; -; Genomic_DNA.
DR   AlphaFoldDB; O97438; -.
DR   SMR; O97438; -.
DR   BindingDB; O97438; -.
DR   ChEMBL; CHEMBL4802003; -.
DR   VEuPathDB; GiardiaDB:DHA2_16453; -.
DR   VEuPathDB; GiardiaDB:GL50581_2343; -.
DR   VEuPathDB; GiardiaDB:GL50803_0016453; -.
DR   eggNOG; ENOG502S00U; Eukaryota.
DR   BioCyc; MetaCyc:MON-11204; -.
DR   BRENDA; 2.7.2.2; 2401.
DR   UniPathway; UPA00996; UER00366.
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   Arginine metabolism; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..317
FT                   /note="Carbamate kinase"
FT                   /id="PRO_0000185152"
SQ   SEQUENCE   317 AA;  34221 MW;  618ACECC085BD881 CRC64;
     MSAGKTVVIA LGGNAMLQAK EKGDYDTQRK NVEIAASEIY KIHKAGYKVV LTSGNAPQVG
     AIKLQNQAAA GVSPEMPLHV CGAMSQGFIG YMMSQAMDNV FCANNEPANC VTCVTQTLVD
     PKDQAFTNPT KPRWRFYTEQ EAKDLMAANP GKILREDAWP AGWRVVVPSP RPLEIVEYGV
     IKTLIDNNVL VICTNGGGIP CKRENKVISG VDAVIDKDLA TSLLAKTLNS DYLMILTDVL
     NACINYKKPD ERKLEEIKLS EILALEKDGH FAAGSMGPKV RAAIEFTQAT GKMSIITSLS
     TAVDALNGKC GTRIIKD