ID B6YT84_THEON Unreviewed; 813 AA.
AC B6YT84;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=TON_0286 {ECO:0000313|EMBL:ACJ15771.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ15771.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ15771.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ15771.1,
RC ECO:0000313|Proteomes:UP000002727};
RX PubMed=18790866; DOI=10.1128/JB.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.J., Lee J.H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00001186};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP000855; ACJ15771.1; -; Genomic_DNA.
DR AlphaFoldDB; B6YT84; -.
DR STRING; 523850.TON_0286; -.
DR KEGG; ton:TON_0286; -.
DR PATRIC; fig|523850.10.peg.288; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.90.870.50; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR041440; HypF_C.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR NCBIfam; TIGR00143; hypF; 1.
DR PANTHER; PTHR42959; CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR42959:SF1; CARBAMOYLTRANSFERASE HYPF; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF17788; HypF_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 46..133
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 243..429
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 813 AA; 91796 MW; 4FB98690BAFEBA61 CRC64;
MQHLLQIWGF VLTPKVQNSF QVFNFWFQKP IKTVKTKKKA VRGMKAYRLH VQGIVQAVGF
RPFVYRIAHE HGLRGYVKNL GDAGVEIVVE GPEKDIGAFL LDLREKLPPL AKIEKIKKRE
IPIQGFDRFY IEKSSQGGSG GDSIIPPDIA ICEDCLRELF DPTNKRYMYP FIVCTNCGPR
FTIIEDLPYD RVNTTMREFP MCDFCESEYK DPLNRRYHAE PVCCPVCGPS YRLYTNDGEE
LIGDPLKKAA ELIDNGYIVA IKGIGGIHLA CDATREDVVA ELRKRIHRPQ KPFAIMAKDV
ETIEEFAFIS PEELEELKSY RRPIMTLRKK EPFPLPENLA PGLHTIGVML PYAGTHYILF
HYSKTPVYVM TSANYPGMPM VKDNERAFEE LKDVADYFLL HNRKILNRAD DSVVRFVNGR
RAVIRRSRGF VPLPIEIPFD YRGLAVGAEL MNAFGVTKNG KIYPSQYIGN TSKVEVLEFM
REAVEHFKRI LRVRDFDLIV ADLHPGYNTT KLAMEMANEL GVEFLQVQHH YAHIASIMAE
HNLDEIVGIA VDGVGYGTDG HTWGGEVIYL SYEDVERLAH IDYYPLPGGD LASYYPLRAL
MGILSKVYGI EELEEVIEKC CPKAIESLRY GKVEFNVVLT QLAKEVNTSY ASSTGRVLDA
FSVLLNVAYR RHYEGEPAMK LESFAIRGKN DLGFSVPVEG ELIKVEELFQ QALEINASPA
DVAYSVHLAL GRAFAEIAVE KAKEFGVKNV GISGGVAFNE LIVKTVRKIV EANGLRFYST
YEVPRGDNGI NVGQAFLGGL YLEGYLTKED LML
//
