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Database: UniProt
Entry: A0A0S8DKW5_9BACT
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ID   A0A0S8DKW5_9BACT        Unreviewed;       751 AA.
AC   A0A0S8DKW5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=AMK70_00850 {ECO:0000313|EMBL:KPK36863.1};
OS   Nitrospira bacterium SG8_35_1.
OC   Bacteria; Nitrospirota; Nitrospiria.
OX   NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK36863.1, ECO:0000313|Proteomes:UP000052010};
RN   [1] {ECO:0000313|EMBL:KPK36863.1, ECO:0000313|Proteomes:UP000052010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK36863.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK36863.1}.
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DR   EMBL; LJTK01000005; KPK36863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DKW5; -.
DR   PATRIC; fig|1704024.3.peg.1080; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000052010; Unassembled WGS sequence.
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; IPR017968; Acylphosphatase_CS.
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; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 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   Transferase {ECO:0000313|EMBL:KPK36863.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          2..88
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          199..384
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   751 AA;  84041 MW;  3C7CBA2DF02D07E1 CRC64;
     MRIRVHINGV VQGVGFRPFV FRLANELGLK GYVLNHPEGV SVEAEGEKKK LYEFLVRVEK
     EKPAIAKIYS LQYAFLEATG ADSFEIRVSN DAGERKVSIL PDIAVCDECM HEVTDPKDRR
     FIYPFTNCTN CGPRYTIIQS LPYDRKNTSM KSFVMCPDCE KEYTLASFRR FHAQPNACHE
     CGPWITLHDC DGQLSSEKSN ALEKVTNLIR KGYIIAVKGI GGYHLVCDAE SNEAVQRLRE
     RKQREEKPMA VMFPDLDSIM KEAVITPIEA RALASIERPI VIVRKKDEST LAPSVSPDNS
     TVGVFLPYTP LHHLIARKLK KPVVATSANV SDDPIVKDEP DAFARLSKIA DYFLTHNRDI
     IRQCDDSVVR IIAERQVPIR RSRGFAPLPI QVPFQFRKPV LALGPSMNNT IAAGIDNKVY
     LSQHIGDLDS PLAIEFYEET IHDFLRLLDI QPEIVVSDLH PGYYSTKFGE KHFDRKLVRV
     QHHFAHILSC LTDNSVPEET EVIGFAFDGT GYGPDGTVWG SEVFIASYSG FKRAYHLRPF
     RLPGGDRSVR EPCRTALSLL YETFGDAALN IRHNPLSDKE KSFLIEMIKK EVHSPVTTGM
     GRLFDGVASL INVKQKISYH AQAAIALEQA ALKSDRTDSY PFRVSNDEID QRAVIEAIVK
     DVDKDTAPEI IARKFHNTIV DIVVSIAESL RKETGIATVA LTGGVFQNAL LSENSFERLT
     EKGFTPLLHQ LVPPNDGGIA LGQTVYGQFL A
//
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