ID I0ELB2_HELC0 Unreviewed; 755 AA.
AC I0ELB2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=HCW_02240 {ECO:0000313|EMBL:AFI03731.1};
OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI03731.1, ECO:0000313|Proteomes:UP000005010};
RN [1] {ECO:0000313|Proteomes:UP000005010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003479; AFI03731.1; -; Genomic_DNA.
DR RefSeq; WP_014660603.1; NC_017737.1.
DR AlphaFoldDB; I0ELB2; -.
DR STRING; 182217.HCW_02240; -.
DR KEGG; hce:HCW_02240; -.
DR PATRIC; fig|182217.3.peg.465; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_7; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000005010; 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; 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; 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 8..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 199..383
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 755 AA; 86192 MW; 2FA864E54CE9481A CRC64;
MCNDATILNK ITLFGVVQGV GMRPFVVALA QKLELVGFVR NVSTALEIVL PKNKTELFLN
ALKNGLPPLA LIEKIEISPY NKVLNFNGFK ILKSKTNALN LLSQIPKDLG VCKNCLHEIR
DKNSPYFHYA FNSCAKCGAR YSLLNALPYD RENSALKPFK LCEFCSSIYK DPTNKRFHIQ
GISCQKCGIT LNYKELKNYD ALLECAKDIQ KGKIIAFKGL GGFAFVCDAR NQVTIERLRL
LKNRPLKPFA LMLKDLNTAH QYVFLNKLEC ESLNSFNAPI LLAHKKTNTQ LAPNIAPNSP
FYGVVLPYTP LHALLLDLLD FPTIFTSANF SSQPLASNEE EIKKLHFLYD FKLTHNRFII
HRIDDSITQC VDNKIRLVRL ARGFAPLYIT LPKPLKKKEK ILALGAEQKG HFSLLDSETS
TLLLSPFCGD LSVLENENHF KETLNFILNA YHFKPTLLAC DKHPNYATTK MALNFNMPLL
QVQHHHAHFL ASILDAFLQD RNTNQFIGII WDGSGAYENK IYGAECFIGD FKEIREVARF
EEFLLLGGEK AIKEPKRLVL EIALKYQLGK LLKRIQKHFN KNELEIFKQM HVRQIQSIAT
NSIGRLFDIV AFSLNLVETI SFEAQSGQVL ENLAKESNET SIYPFEIKDN MVRLRKFYQA
FENDLEKLEF KHIAKKFFNS LVEIIIALIM PFKEHAVVFG GGVFCNKLLC EQLAKRLKEL
KRKYFFHKNF PPNDSNIAIG QALMAYYQTQ IIKKD
//
