ID B9AF89_METSM Unreviewed; 750 AA.
AC B9AF89;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:EEE42129.1};
GN ORFNames=METSMIALI_01033 {ECO:0000313|EMBL:EEE42129.1};
OS Methanobrevibacter smithii DSM 2375.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=483214 {ECO:0000313|EMBL:EEE42129.1, ECO:0000313|Proteomes:UP000003489};
RN [1] {ECO:0000313|EMBL:EEE42129.1, ECO:0000313|Proteomes:UP000003489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2375 {ECO:0000313|EMBL:EEE42129.1,
RC ECO:0000313|Proteomes:UP000003489};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEE42129.1, ECO:0000313|Proteomes:UP000003489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2375 {ECO:0000313|EMBL:EEE42129.1,
RC ECO:0000313|Proteomes:UP000003489};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Methanobrevibacter smithii (DSM 2375).";
RL Submitted (NOV-2008) 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}.
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:EEE42129.1}.
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DR EMBL; ABYW01000007; EEE42129.1; -; Genomic_DNA.
DR RefSeq; WP_004035896.1; NZ_DS996911.1.
DR AlphaFoldDB; B9AF89; -.
DR PATRIC; fig|483214.13.peg.991; -.
DR HOGENOM; CLU_009164_0_0_2; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000003489; 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; 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; 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:EEE42129.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..87
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 196..381
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 750 AA; 84025 MW; A67C0072A90DB43C CRC64;
MMAKKILTQG IVQGVGFRPY IYRLAKDLNL NGYVRNLGNV VEIILEGDNI DLFIDRLPKE
LPPIAKIDSM KTEDIAREGF DDFTIIESSD EFSGVSVIPP DIAICDSCLE EIRNPKDRRY
KYPFNACTDC GPRFTVIDSV PYDRVRTSMD EFPLCDSCLE EYGEPLNRRY HGEAICCSDC
GPQMKICKGP EEINSNNPIK VAADKLKEGK IIAIKGIGGT HLVVDAYNDK AVKELRKRLN
RPNQAFAVMS KDLDSVKGYA KLSKKEIATI TSNKRPIVVL KKNDNYNFPE SLAPGLHNIG
VMLPYSPMHY LLFDEGDIDT YVMTSANTPG EPMMITNKDI LNLNGISDYS LIHNRKILNR
CDDSVIRFRN DTLSFIRRSR GYTPEPYKIN YDVNDLNVLA LGPELDVTFA MAKDNMIYPS
QHIGNTNKLK TLKFMKEAIE NMKRITKINY FDAIACDLHP HFFTTKLAHE FSDEFGCDVI
GVQHHHAHSI ALANDYSIDE MIVIACDGVG YGSDAASWGG EILYTNITDF ERLGHLQAHK
MPGGDMATKH PIRMLLSIID DEDLISKYVD YFKYGETEIK NIYRQLEAGI NVGLTTSTGR
VLDSVSAALE ICNTRTYEGE CSMKLESVAY YSKNDIEIPF EIKDNILNTR EILREVVRLY
QKGENKSDIA NAAQKTIAKG LSQIAIENAD KKGVDVIGAT GGVFYNEAIT DTCKKYIEEN
GYNFIQHKNT CAGDGSVSLG QAIVAKTKLN
//
