ID A0A151FDH1_9EURY Unreviewed; 752 AA.
AC A0A151FDH1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=AYK18_00235 {ECO:0000313|EMBL:KYK38930.1};
OS Theionarchaea archaeon DG-70.
OC Archaea; Euryarchaeota; Theionarchaea.
OX NCBI_TaxID=1803813 {ECO:0000313|EMBL:KYK38930.1, ECO:0000313|Proteomes:UP000075311};
RN [1] {ECO:0000313|Proteomes:UP000075311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL Submitted (FEB-2016) 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:KYK38930.1}.
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DR EMBL; LSSB01000001; KYK38930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151FDH1; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000075311; 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; 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; 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 44..130
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 228..405
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 752 AA; 84692 MW; D94840B661D3A1CF CRC64;
MIIYSGIVPK RLHITEEVDV SAKCISFLTE NQKEFKRLTI QKSMLRLQVH GIVQAVGFRP
FVHRIAVKHN ITGFIANVGD HVEIAAQGTP ENIEQFLNDL KNKKPPISEI DRIEKEILPD
QQFKEFEVIK SKKREGGESI IPPDIAVCNN CLKELFSPRD KRYLYPFINC THCGPRFTII
EEMPYDREKT SMSAFPMCDF CHQQYTDIAD RRYHAEPVCC PEQGPHYTMS TAKAADLIDQ
GGIVAVKGLG GFHIACKIND PVVLRLRTLL KRPQQPFALM ARNLESVKKI AYTSEQEEKL
LQSWMRPIVV LPKKEPLKNE APLLHTIGVM LPYAPVHHLI FHHCASDVLV MTSANFPGNP
MIIDNDTAER ELSFVDAFLY HNLEIVNRCD DSVIRNEVFL RRSRGFVPKG IPISHTTVVL
AVGGELNNTF CLTKGGKAFL SQHIGDTSNY DTLLFQKEAI NHFMRLLVLK WEDINTIVCD
MHPQYNTRNQ AEAFAEQYGI PLKMVQHHYA HAYGLMAEHD KEMMVITADG AGYGLDGHVW
GGEVLFKNER LGHLEYVPML GGDLATKYPE RMLLSYIEHE IPGHRYSKGE QRVLLNQLQK
EKVLTSSTGR FLDAVAAFLG VCYERTYEGE PAMKLESLAL RGDSLDIEME VEGDCIMVKD
FVKEISRLKA SKKDVAKTAH TALGKAYMEL ASGVNDMHVP VGFSGGVAYN EIVTNVLQKE
AKKRGITFYV HRLVPPGDGG TSFGQVASIP TE
//
