ID D7DUS4_METV3 Unreviewed; 830 AA.
AC D7DUS4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=Mvol_1227 {ECO:0000313|EMBL:ADI36884.1};
OS Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36884.1, ECO:0000313|Proteomes:UP000007722};
RN [1] {ECO:0000313|EMBL:ADI36884.1, ECO:0000313|Proteomes:UP000007722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanococcus voltae A3.";
RL Submitted (MAY-2010) 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; CP002057; ADI36884.1; -; Genomic_DNA.
DR AlphaFoldDB; D7DUS4; -.
DR STRING; 456320.Mvol_1227; -.
DR KEGG; mvo:Mvol_1227; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR InParanoid; D7DUS4; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000007722; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007722};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 2..104
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 216..401
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT COILED 419..446
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 17
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 830 AA; 94503 MW; 4CEF237DDF4BDCF2 CRC64;
MLKKIFVSGI VQGVGFRPFV YNIAKKNNLK GYVKNKGNFV EIVVNGNLKD INNFLINLKE
EKPVLSKINK LEIEDIDTNN DLDNDLNNKL DGLEELNKEF HIYSSQNVNN EVAGTIPPDI
ALCDDCIKEL KDKKDIRYEY PFIACVNCGP RFTVIKKLPY DRENTSMDKF PLCENCEKEY
KNPNDRRFHA QANCCDKCGP KVFLTDSNGN KLLEKESAIK KAVELLEDGK ILAIKGIGGT
HLVCDANNDD AILELRKRLN RPTQAFAIMS TEEKYPLFSK FTKIEEEALN SYRRPIVALK
KKENGYNKYI SENISNLDTV GVMLPYSGLH YLLFGKCTAY VMTSANLPGL PMAITNDKII
ESLKDIADYF LLHNRDIVNR CDDSVLKLIS NRMMILRRSR GYAPEPIEID FSKMAEFENK
NKYKNKDENE NENKEIINEL NNKKIEKNII SVGAELNSVA CLTKGNKFYM TQYIGNTSKY
ETYNYLKDAV HNILRLTNTN KLDTIVCDLH PQFNSKKFAN ELTKEYDAPM FEIQHHAAHV
YSLMGDNGFF EPNITIALDG LGYGKDGNIW GGELLYCDKN YEIHRIGHLE EQLQLGGDLS
TKYPLRMLFS ILSKKMSLDE SFEFVKKYIG KYPELTEKEL KLIKMQIKSG LNTAITTSTG
RVLDSVAALL SVCFKKTYDG EPSIRLEAFA NSCDEKEKKQ ILEFVENMDN IRYSRLIDYE
NNIIKTSEIV YDCYTLLQNE VFSKKGIAYY AHLVLANCLC IISENSAKKL NINTLGLTGG
VSYNRIITEY MVIKLKNKGF NILLHNNVPN GDGGIAFGQS VGYILKNEIN
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