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Database: UniProt
Entry: I6TVJ5_9EURY
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Original site: I6TVJ5_9EURY 
ID   I6TVJ5_9EURY            Unreviewed;       773 AA.
AC   I6TVJ5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=PFC_01925 {ECO:0000313|EMBL:AFN03354.1};
OS   Pyrococcus furiosus COM1.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=1185654 {ECO:0000313|Proteomes:UP000006216};
RN   [1] {ECO:0000313|EMBL:AFN03354.1, ECO:0000313|Proteomes:UP000006216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM1 {ECO:0000313|EMBL:AFN03354.1,
RC   ECO:0000313|Proteomes:UP000006216};
RX   PubMed=22636780; DOI=10.1128/JB.00439-12;
RA   Bridger S.L., Lancaster W.A., Poole F.L.II., Schut G.J., Adams M.W.;
RT   "Genome Sequencing of a Genetically-Tractable Pyrococcus furiosus Strain
RT   Reveals a Highly Dynamic Genome.";
RL   J. Bacteriol. 194:4097-4106(2012).
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; CP003685; AFN03354.1; -; Genomic_DNA.
DR   RefSeq; WP_014835167.1; NC_018092.1.
DR   AlphaFoldDB; I6TVJ5; -.
DR   GeneID; 41712364; -.
DR   KEGG; pfi:PFC_01925; -.
DR   PATRIC; fig|1185654.4.peg.393; -.
DR   HOGENOM; CLU_009164_0_0_2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000006216; 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; 2.
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          3..90
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          201..387
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   773 AA;  87411 MW;  101186E44648F899 CRC64;
     MKAYRIHVQG IVQAVGFRPF VYRIAHAHNL RGYVRNLGDA GVEIVVEGRE EDIEAFIKDL
     YKKKPPLARI DKVEREEIPL QGFDRFYIEK SSTEKKGEGD SIIPPDIAIC EDCLRELFNP
     TDKRYMYPFI VCTNCGPRFT IIEDLPYDRE NTAMREFPMC EFCRSEYEDP LNRRYHAEPV
     ACPTCGPSYR LYTSDGNEII GDPLRKAAKL IDKGYIVAIK GIGGIHLACD ATREDVVAEL
     RKRIFRPQKP FAIMAKDLET VRTFAYISPE EEEELTSYRR PIVALKKKEP FPLPENLAPG
     LHTIGVMLPY AGTHYILFHW SKTPVYVMTS ANFPGMPMIK DNEEAFEKLR DVADYLLLHN
     RRIPNRADDS VVRFVDGRRA VIRRSRGFVP LGIEIPFEYK GLAVGAELMN AFGVVKNGKV
     YPSQYIGDTS KIEVLEFMRE AVRHFFKILR VDNLDLVVAD LHPSYNTTKL GMEIAEEFGA
     EFLQVQHHYA HVASVMAEHN LEEVVGIALD GVGYGTDGKT WGGEVIYLSY EDVERLAHIE
     YYPLPGGDLA SYYPLRALIG ILSLNHDLEE VEKIIREFCP NAIKSLKYGE TEFRVIMRQL
     SSGINVAYAS STGRVLDAFS VLLNVSYRRH YEGEPAMKLE SFAYQGKNDL KLTAPIEGEE
     IKVSELFEEV LELMGKANPK DIAYSVHLAL ARAFAEVSVE KAKEFGAKTV VLGGGVGYNE
     LIVKTIRKIV EGRGLRFLTT YEVPRGDNGI NVGQAFLGGL YLEGYLNRED LSI
//
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