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Database: UniProt
Entry: T1U7T6_HELPX
LinkDB: T1U7T6_HELPX
Original site: T1U7T6_HELPX 
ID   T1U7T6_HELPX            Unreviewed;       750 AA.
AC   T1U7T6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   Name=hypF {ECO:0000313|EMBL:AGT73299.1};
GN   ORFNames=HPSA20_0054 {ECO:0000313|EMBL:AGT73299.1};
OS   Helicobacter pylori SouthAfrica20.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1352356 {ECO:0000313|EMBL:AGT73299.1, ECO:0000313|Proteomes:UP000015920};
RN   [1] {ECO:0000313|EMBL:AGT73299.1, ECO:0000313|Proteomes:UP000015920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SouthAfrica20 {ECO:0000313|EMBL:AGT73299.1};
RX   PubMed=24072860;
RA   Duncan S.S., Bertoli M.T., Kersulyte D., Valk P.L., Tamma S., Segal I.,
RA   McClain M.S., Cover T.L., Berg D.E.;
RT   "Genome Sequences of Three hpAfrica2 Strains of Helicobacter pylori.";
RL   Genome Announc. 1:e00729-13(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}.
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DR   EMBL; CP006691; AGT73299.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1U7T6; -.
DR   KEGG; hpys:HPSA20_0054; -.
DR   PATRIC; fig|1352356.3.peg.49; -.
DR   HOGENOM; CLU_009164_0_0_7; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000015920; 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   Transferase {ECO:0000313|EMBL:AGT73299.1};
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;  85140 MW;  E1F9556B25D70E15 CRC64;
     MNKITLFGVV QGVGMRPFIY TLAQKLELIG FVCNTQTALE IILPIQKTES FLNALKKELP
     PLALVERIII SPYDKALHFN DFRILESKNH PLNLLSQIPK DLGVCDDCLH EIRDENSPYF
     HYAFNSCAKC GARYSLLNAL PYDRENSALK PFKLCEFCAF VYKDTTNKRF HIQGISCKKC
     GITLNYKQLN DDDALLECAK DIQKGKIIAL KGLGGFALVC DARNFQTIER LRLLKNRPLK
     PFALMFKDLN TAKQYAFLNE LECESLRSAN APILLAHKKP NAQLAPNIAK NSPFYGIILP
     YTPLHALLLD LLNFPIVFTS ANFNSLPLAS DEKELDRFHF IFDFKLTHNR AIIHRIDDSI
     AQCVDNMIRP MRLARGFAPL YLTLPKRSHN APTKILALGA EQKGHFSLLD SETSVLLLSP
     FCGDLSVLEN EKHFKETLNF FLNAYDFKPT LLACDEHKNY TTTKMACEFN APLLQVQHHH
     AHFLASMLDA FLQDPNLNCP FIGIVWDGSG AYENKIYGAE CFVGDFNQIK ETARFEEFLL
     LGGQKAIKDP KRLVLEISLK HQLNKLLKRV QKHFKEDEIE IFKQMHDKEI QSVATNSIGR
     LFDIVAFSLG AVGTISFEAE SGQVLENLAL QSEESAFYPF KIKNSVVGLE EFYQALEKDL
     DILEPKHIAK KFFNSLIEII TALIAPFKEH IVVCSGGVFC NQLLCEQLAK RFKTLQRKYF
     FHKHFPPNDS SIPVGQALMA YFNPTIIKKG
//
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