GenomeNet

Database: UniProt
Entry: V5NK73_HELPX
LinkDB: V5NK73_HELPX
Original site: V5NK73_HELPX 
ID   V5NK73_HELPX            Unreviewed;       750 AA.
AC   V5NK73;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=U064_0048 {ECO:0000313|EMBL:AHA89000.1};
OS   Helicobacter pylori BM012S.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1407463 {ECO:0000313|EMBL:AHA89000.1, ECO:0000313|Proteomes:UP000018543};
RN   [1] {ECO:0000313|EMBL:AHA89000.1, ECO:0000313|Proteomes:UP000018543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM012S {ECO:0000313|EMBL:AHA89000.1,
RC   ECO:0000313|Proteomes:UP000018543};
RX   DOI=10.1371/journal.pone.0082187;
RA   Linz B., Windsor H.M., Gajewski J.P., Hake C.M., Drautz D.I.,
RA   Schuster S.C., Marshall B.J.;
RT   "Helicobacter pylori genomic microevolution during naturally occurring
RT   transmission between adults.";
RL   PLoS ONE 8:E82187-E82187(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006889; AHA89000.1; -; Genomic_DNA.
DR   RefSeq; WP_023591502.1; NC_022911.1.
DR   AlphaFoldDB; V5NK73; -.
DR   KEGG; hez:U064_0048; -.
DR   PATRIC; fig|1407463.3.peg.46; -.
DR   HOGENOM; CLU_009164_0_0_7; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000018543; 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; 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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..86
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          192..376
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        16
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   750 AA;  84754 MW;  B5D15481DD04A6B4 CRC64;
     MNKITLFGVV QGVGMRPFIY TLAQKLELVG FVRNAQVALE IVLPAHQTES FLNALKKESP
     PLALVEKIII SPYDKALHFN DFRILESKNH PLNLLSQIPK DLGVCEDCLR EIRDKNSPYF
     YYAFNSCAKC GARYSLLNAM PYDRENSALK PFKLCEFCAS VYQDPTNKRF HIQGISCKKC
     GIALNYKRFK NDDALLECAK DIQKGKIIAL KGLGGFALLC DGRNFQTIER LRLLKNRPLK
     PFALMFKDLN TAKQHAFLNA SEGESLISAS APILLARKKP DTPLAPNIAK NSPFYGVILP
     YTPLHALLLD LLDFPIVFTS ANFSSLPLAS DEAEIDSLSF IFDFKLTHNR AIIHRIDDSI
     AQLVDNAIRP MRLARGFAPL YLALPKRSNG SPKKILALGA QQKGHFSLLD SETSILLLSP
     FCGDLSVLEN EKHFKETLNF FLKTYDFKPT ILACDKHQNY TTTKMACGFN TPLLQVQHHH
     AHFLASVLDA LLQDPHLNHP FIGIVWDGSG AYENKVYGAE CFVGDFERIE EVARFEEFWL
     LGGQKAIKEP KRLVLEISLK HQLNKLLKRV QKHFKEDELE IFQQMHDRKI QSIATNSIGR
     LFDIIAFSLD LTGTISFEAE SGQVLENLAL QSDEIAFYPF TIKNSVVCLK EFYQAFEKDL
     GVLEPERIAK KFFNSLVEII TALIAPFKEH VVVCSGGVFC NQLLCEQLAK RLRGLKRQYF
     FHKHFPPNDS SIPIGQALMA YFNPTIIKKG
//
DBGET integrated database retrieval system