ID A6VIC9_METM7 Unreviewed; 769 AA.
AC A6VIC9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=MmarC7_1139 {ECO:0000313|EMBL:ABR66205.1};
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368 {ECO:0000313|EMBL:ABR66205.1};
RN [1] {ECO:0000313|EMBL:ABR66205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:ABR66205.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) 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; CP000745; ABR66205.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VIC9; -.
DR STRING; 426368.MmarC7_1139; -.
DR KEGG; mmz:MmarC7_1139; -.
DR eggNOG; arCOG01187; Archaea.
DR HOGENOM; CLU_009164_0_0_2; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
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 3..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 201..387
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 769 AA; 86401 MW; 60FF931E0C0D1222 CRC64;
MTTKRIDVKG IVQGVGFRPF VYRIAKKNDM QGYVKNMGNY VEIVVSGELK NIDAFLSDLK
LEKPPLSKID SISIKNIDEN LNEIYSDFTI TLSENSEIEE EGTIPPDISI CDECLKEIMD
KTDRRSNYAF TACTNCGPRF TVIEKLPYDR ENTSMKDFPL CENCIEEYKS PENRRFHAQA
TCCEFCGPEL FITNNSGKIV SNDIVDAVKF LENGKILAIK GIGGTHLVCS INSDETVLEL
RKRLNRPTQA FAIMSREEYL DLFSKIDENE LNAIKSPKKP IVALKKNELY GKYFSKHVSN
LNTIGVMLPY SGLHHLLFEN TDQIAYIMTS ANMPGLPMSI DNEQILEKLG NIADYFLLHN
RKIVNRCDDS VLKEINGKME LLRRSRGFAP EPVEVNYGTI KNSNKNILAL GPELNSVACL
VKNNKFYLTQ YIGNTGKYET FNYLKEAVEN LIKITNTNKI DTIVCDLHPS FNSTIFAKEL
GEKYGIPVTQ IQHHESHCYS LMGDSDIFEN NVTIAIDGLG YGNDGNIWGG EIFLFKDGKI
ERTGHLEEQI QPGADLASKY PLRMLASVLH KANLNVSEII KGYNYFSEKE LKLILFQLEK
NINVSKTTST GRILDSISAL VSLCFERTYD GEPSIRLEAL ANAYNGKISE IETLVEDSLK
IENNIIDTTS LIVKSLEMLN NNEKIEKIAY FIHIALADGL SKIAIETAKK QGIEYIGITG
GVSYNKIISE RIVEKIEKES LKPLIHERIP NGDGGISFGQ AIGYLLNSN
//
