ID H8H6N4_HELPX Unreviewed; 750 AA.
AC H8H6N4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=HPELS_00235 {ECO:0000313|EMBL:AFF19635.1};
OS Helicobacter pylori ELS37.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055527 {ECO:0000313|EMBL:AFF19635.1, ECO:0000313|Proteomes:UP000007885};
RN [1] {ECO:0000313|EMBL:AFF19635.1, ECO:0000313|Proteomes:UP000007885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ELS37 {ECO:0000313|EMBL:AFF19635.1,
RC ECO:0000313|Proteomes:UP000007885};
RA Bertoli M.T., Kersulyte D., Pascasio M.A., Berg D.E.;
RL Submitted (JUL-2011) 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; CP002953; AFF19635.1; -; Genomic_DNA.
DR RefSeq; WP_014419480.1; NC_017063.1.
DR AlphaFoldDB; H8H6N4; -.
DR KEGG; hpe:HPELS_00235; -.
DR PATRIC; fig|1055527.3.peg.44; -.
DR HOGENOM; CLU_009164_0_0_7; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000007885; 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; 85002 MW; 2CF42596C1DF48E0 CRC64;
MNKITLFGVV QGVGMRPFVY TLAQKLGLVG FVRNTQAALE VVLPAHKTES FLNALKKGLP
PLALVEKITI SPYDKALHFN DFRILESKNH PLNLLSQIPK DLGVCKDCLH EIRDKNSPYF
HYAFNSCAKC GARYSLLNAM PYDRENSALK PFKLCKFCAS VYKDANNKRF HIQGISCKKC
GIALNYKRFK NDDALLECAK DIQKGKIIAL KGLGGFALLC DARNFQTIER LRLLKNRPLK
PFALMFKDLK SAKQHAFLNA LECESLISAS TPILLVHKKP DTQLAPNIAK NSPFYGVILP
YTPLHALLLD LLDFPIVFTS ANFNSLPLAS DEKEIDSLHF IFDFKLTHNR AIIHRIDDSI
AQRMDNAIRP MRLARGFTPL YLTLPKRSFN VPKKILALGA EQKGHFSLLD SETSILLLSP
FCGDLSVLEN EKHFKETLNF FLKTYDFKPT LLACDKHKNY TTTKMAFKVN TPLLQVQHHH
AHFLASVLDA LLQDSHLNHP FIGIVWDGSG AYDNKIYGAE CFVGDFERIE EVARFEEFWL
LGGQKAIKEP KRLVLEIALK HQLNKLLKHV QKHFKEDELE IFKQMHDKKI QSVATNSIGR
LFDIVAFSLD LTGTISFEAE SGQVLENLAL QSDESAFYPF TIKNSVVGLK EFYQAFEKDL
GVLEPKRIAK KFFNSLIEII TALIAPFKEH VVVCSGGVFC NQLLCEQLAK RLKKLQRQYF
FHKHFPPNDS SIPVGQALMA YFNPTIIKKG
//
