ID I7H4J2_9HELI Unreviewed; 827 AA.
AC I7H4J2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:BAM31810.1};
GN ORFNames=HCBAA847_0568 {ECO:0000313|EMBL:BAM31810.1}, HCCG_00912
GN {ECO:0000313|EMBL:EFR46365.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31810.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:EFR46365.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 18818 {ECO:0000313|EMBL:EFR46365.1};
RG The Broad Institute Genome Sequencing Platform;
RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Helicobacter cinaedi strain CCUG 18818.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAM31810.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31810.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
RN [3] {ECO:0000313|EMBL:BAM31810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31810.1};
RA Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000005755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 18818 {ECO:0000313|Proteomes:UP000005755};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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; AP012492; BAM31810.1; -; Genomic_DNA.
DR EMBL; DS990392; EFR46365.1; -; Genomic_DNA.
DR RefSeq; WP_002956223.1; NZ_DS990392.1.
DR AlphaFoldDB; I7H4J2; -.
DR KEGG; hcb:HCBAA847_0568; -.
DR PATRIC; fig|1206745.3.peg.595; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_7; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000005755; Unassembled WGS sequence.
DR Proteomes; UP000006036; Chromosome 1.
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; 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; 1.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 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 19..107
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 242..444
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 827 AA; 93094 MW; F1605A9908B2F427 CRC64;
MKNADKLPKP NTHIDAKTAY AIELFGIIQG VGFRPFVYQV ATSLNLKGYV QNRYNSLYIY
LESTLIQSEQ FLQEILQNPP PNAVIHAHTM HQVPFVTPPY SDFRILASST EKQDDKLFLP
QDVAICQACL QDMGCNTGQD IKQDTKQNSR QNPRFQDYAF TTCSYCGARH SIIHALPYDR
TNTSMREFKK CKDCEREYHT PTNRRFHAQP ISCNQCAIRM RLIIPSLKQS YIFAYPKATS
DILLLALVAQ KIMEGKIIAI KGIGGFNLIA SATNIQAIMS LKKRKNRSKK PFAIMFKNLQ
DIASVAEINE SERQALLSPQ APIVLLNKHF HNRQHNRSHN KRENAILSSQ ALELIAPQVS
SIGAILPYNG IMHLLFRFLN TPLIFTSANV SGTPIITKLD ELMEKLSGVF DMVLDYDREI
THALDDSIMR FMAGELRPLR LSRGFTPLFL PFGSKKLCLS LGAQQKSSLS IVYKNTLISP
YFGDLHNVDS ICRYEKELQF FLSLYVNKPK VIVSDLHPQY ASTHLAKNLT NNTALLDSAT
DSATSLDSPQ FLQISHHKAH FYAILAESNA LNNDGFGIIW DGTGLGEDGG IWGGEGFIYD
SKHKSMSRIF SLKPFALLGG EGSIKEIGRL ALGLLWSYGI QTQNLATKNI EKRENISLLQ
NAFESKVFLQ TSSMGRLIDC VACLLGILEV QSYEGQSGAL LESYALRERA EVSPYPFKID
NGEIDCKAMI EEILKTQDKA KGAKRFLETL AYMALEMSEK VLKTKRVRVY FSGGVFQNKF
LCDRIHTLFK EHNIPFYMHK ILPCNDFSIS FGQAVCGSME QNKGDVK
//
