ARCC_HALSA
ID ARCC_HALSA Reviewed; 307 AA.
AC Q48295; Q9HHM9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Carbamate kinase;
DE Short=CK;
DE EC=2.7.2.2;
GN Name=arcC; OrderedLocusNames=VNG_6316G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC200.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=R1 / S9 / L33;
RX PubMed=8759859; DOI=10.1128/jb.178.16.4942-4947.1996;
RA Ruepp A., Soppa J.;
RT "Fermentative arginine degradation in Halobacterium salinarium (formerly
RT Halobacterium halobium): genes, gene products, and transcripts of the
RT arcRACB gene cluster.";
RL J. Bacteriol. 178:4942-4947(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC200;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- FUNCTION: Carbamate kinase involved in the arginine deiminase pathway
CC of fermentative arginine utilization. {ECO:0000269|PubMed:8759859}.
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 Evidence={ECO:0000269|PubMed:8759859};
CC -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate
CC degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: 20-fold induction in fermentatively grown cells.
CC {ECO:0000269|PubMed:8759859}.
CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR EMBL; X80931; CAA56905.1; -; Genomic_DNA.
DR EMBL; AE004438; AAG20947.1; -; Genomic_DNA.
DR PIR; T44864; T44864.
DR RefSeq; WP_010904160.1; NZ_BK010831.1.
DR AlphaFoldDB; Q48295; -.
DR SMR; Q48295; -.
DR EnsemblBacteria; AAG20947; AAG20947; VNG_6316G.
DR GeneID; 5954931; -.
DR GeneID; 62888215; -.
DR KEGG; hal:VNG_6316G; -.
DR PATRIC; fig|64091.14.peg.2293; -.
DR HOGENOM; CLU_076278_0_0_2; -.
DR InParanoid; Q48295; -.
DR OMA; QPMDVAG; -.
DR OrthoDB; 77437at2157; -.
DR PhylomeDB; Q48295; -.
DR BioCyc; MetaCyc:MON-663; -.
DR UniPathway; UPA00996; UER00366.
DR Proteomes; UP000000554; Plasmid pNRC200.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008804; F:carbamate kinase activity; IBA:GO_Central.
DR GO; GO:0019546; P:arginine deiminase pathway; IBA:GO_Central.
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; Cytoplasm; Kinase; Nucleotide-binding;
KW Plasmid; Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Carbamate kinase"
FT /id="PRO_0000185142"
SQ SEQUENCE 307 AA; 32535 MW; B8E58C81ED7B8435 CRC64;
MSYTVVALGG NALLRGGEGS IQDQRDTIEQ TVPHFVDLYE RGHELVFTHG NGPQVGQLLL
QNEEAESAAE KPLDVLGAES QAQIGYLLQQ QLREELGETP ATVITQTIVD EDDPAFDDPT
KRIGPFYDED EASEKDFPVK EGTDGDGNVG YRRVVPSPKP VDIVEAEHIK TLVETGKPVI
SSGGGGVPVV EDGDSLTGVA AVIDKDRAAQ SLATDIGADE FLVLTDVDAV YRNFGTEDEE
ELSELTTEEA ADMLAAGEFG EGSMAPKVEA CIEFVESGGD RAIITKPETA TEALDGAAGT
TVVPADE