ID J0KSM1_HELPX Unreviewed; 750 AA.
AC J0KSM1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:EJB53650.1};
GN ORFNames=HPHPH27_0269 {ECO:0000313|EMBL:EJB53650.1};
OS Helicobacter pylori Hp H-27.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992040 {ECO:0000313|EMBL:EJB53650.1, ECO:0000313|Proteomes:UP000003693};
RN [1] {ECO:0000313|EMBL:EJB53650.1, ECO:0000313|Proteomes:UP000003693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-27 {ECO:0000313|EMBL:EJB53650.1,
RC ECO:0000313|Proteomes:UP000003693};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(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 -!- 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:EJB53650.1}.
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DR EMBL; AKOH01000001; EJB53650.1; -; Genomic_DNA.
DR RefSeq; WP_001879393.1; NZ_AKOH01000001.1.
DR AlphaFoldDB; J0KSM1; -.
DR PATRIC; fig|992040.3.peg.261; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000003693; 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:EJB53650.1};
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..373
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; 84880 MW; 7D98F63F6A60A791 CRC64;
MNKITLFGVV QGVGMRPFIY TLAQKLELAG FVRNTQAALE VILPAHKTES FLNALKKGLP
PLALVEKITI SPYDKALHFN GFRILESKNH PLNLLSQIPK DLGVCKDCLC EIRDKNSPYF
YYAFNSCAKC GARYSLLNAL PYDRENSALK PFKLCEFCAS VYQDPTNKRF HIQGISCKKC
GIALNYKRFK NDDALLECAK DLQRGKIIAL KGLGGFALLC DGRNFQTIER LRLLKNRPLK
PFALMFKDLN SAKQHAFLNA LECESLSSIS APILLARKKP NTQLAPNIAK NSPFYGVILP
YTPLHALLLD LLDFPIVFTS ANFSSLPLAS DEAEIDALSF IFDFKLTHNR TIIHRIDDSI
VQRVDNIIRP MRLARGFAPL YLTLPKRSNH PPKKILALGA EQKGHFSLLD SETSVLLLSP
FCGDLSVLEN EKHFKETLNF FLKTYDFKPT LLACDKHQNY TTTQMAFEFN TPLLQVQHHH
AHFLASVLDA LLQNPHLNHP FIGIIWDGSG AYDNKVYGAE CFVGDFEYIE EVARFEEFWL
LGGQKAIKEP KRLVLEIALK HQLNKLLGRV QKHFKEDELE IFKQMHDKKI QSVATNSIGR
LFDIVAFSLD LTGTISFEAE SGQVLENLAL QSDEIAFYPF KIKNSVVGLK DFYQAFEKDL
GVLEPERIAK KFFNSLVEII TALIVPFKEH VVVCSGGVFC NQLLCEQLAK RLRGLKRQYF
FHKHFPPNDS SIPIGQALMA YFNPTIIKKG
//
