CPKA_PYRAB
ID CPKA_PYRAB Reviewed; 314 AA.
AC Q9UWF8; G8ZI47;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Carbamate kinase;
DE EC=2.7.2.2;
DE AltName: Full=Carbamate kinase-like carbamoylphosphate synthase;
GN Name=cpkA; Synonyms=cpa; OrderedLocusNames=PYRAB08820; ORFNames=PAB0593;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=11523892; DOI=10.1007/s007920100201;
RA Purcarea C., Herve G., Cunin R., Evans D.R.;
RT "Cloning, expression, and structure analysis of carbamate kinase-like
RT carbamoyl phosphate synthetase from Pyrococcus abyssi.";
RL Extremophiles 5:229-239(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR EMBL; AF081680; AAF23075.1; -; Genomic_DNA.
DR EMBL; AJ248285; CAB49796.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70288.1; -; Genomic_DNA.
DR PIR; C75135; C75135.
DR RefSeq; WP_010868005.1; NC_000868.1.
DR AlphaFoldDB; Q9UWF8; -.
DR SMR; Q9UWF8; -.
DR STRING; 272844.PAB0593; -.
DR EnsemblBacteria; CAB49796; CAB49796; PAB0593.
DR GeneID; 1496232; -.
DR KEGG; pab:PAB0593; -.
DR PATRIC; fig|272844.11.peg.932; -.
DR eggNOG; arCOG00863; Archaea.
DR HOGENOM; CLU_076278_0_0_2; -.
DR OMA; QPMDVAG; -.
DR OrthoDB; 77437at2157; -.
DR PhylomeDB; Q9UWF8; -.
DR BRENDA; 6.3.4.16; 5242.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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:InterPro.
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 InterPro; IPR023000; Shikimate_kinase_CS.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..314
FT /note="Carbamate kinase"
FT /id="PRO_0000185148"
SQ SEQUENCE 314 AA; 34355 MW; 85DED48E6A01A8B2 CRC64;
MPERVVIALG GNALQQRGQK GTYEEMMENV KKTAKQIAEI IARGYEVVIT HGNGPQVGTI
LLHMDAGQSL HGIPAQPMDV AGAMSQGWIG YMIQQALRNE LRKRGIEREV VTIVTQTIVD
KDDPAFENPT KPVGPFYDEE TAKKLAKEKG WVVKEDAGRG WRRVVPSPDP KRHVEAETIK
KLVEDGVIVI ASGGGGVPVI EEDGEIKGVE AVIDKDLAGE RLAEEVNADI LMILTDVNGA
ALYYGTEKET WLREVKVDEM ERYYQEGHFK AGSMGPKVLA AIRFVKNGGK RAIIAHLEKA
VEALEGKTGT QVIP