ID A0A1D2X193_9EURY Unreviewed; 777 AA.
AC A0A1D2X193;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=NL43_06825 {ECO:0000313|EMBL:OED29694.1};
OS Methanosphaera sp. WGK6.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1561964 {ECO:0000313|EMBL:OED29694.1, ECO:0000313|Proteomes:UP000094737};
RN [1] {ECO:0000313|EMBL:OED29694.1, ECO:0000313|Proteomes:UP000094737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WGK6 {ECO:0000313|EMBL:OED29694.1,
RC ECO:0000313|Proteomes:UP000094737};
RX PubMed=27022996; DOI=10.1038/ismej.2016.41;
RA Hoedt E.C., Cuiv P.O., Evans P.N., Smith W.J., McSweeney C.S., Denman S.E.,
RA Morrison M.;
RT "Differences down-under: alcohol-fueled methanogenesis by archaea present
RT in Australian macropodids.";
RL ISME J. 10:2376-2388(2016).
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:OED29694.1}.
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DR EMBL; JRWK01000013; OED29694.1; -; Genomic_DNA.
DR RefSeq; WP_069593306.1; NZ_JRWK01000013.1.
DR AlphaFoldDB; A0A1D2X193; -.
DR STRING; 1561964.NL43_06825; -.
DR PATRIC; fig|1561964.3.peg.1363; -.
DR OrthoDB; 371970at2157; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000094737; 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; IPR017968; Acylphosphatase_CS.
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; 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 5..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 203..389
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 777 AA; 86945 MW; 7348BA119A05F972 CRC64;
MKEYTAQLLV DGIVQGVGFR PTVYRLAKVM NLTGYVRNMG NIVEILIQGT YDDIQLFVDE
LQEHKPIRSE INSINLDIRE EVTSTTRYND FTILNSSDEL SGSAVIPPDM TICDECLEEI
VDLNNHHYYY PFTACTNCGP RFTVIDQVPY DRKNTTMDEF PLCNHCAKEY SNPLDRRYHA
EATCCPDCGP QVFLYNDEHI PSQDPIRDAS KLIDEGNILA IKGIGGTHLV CKTSTDDAID
KLRERLGRKT QPFACMTPDV ETAKLFVEFS DDEKKMLESV SRPIVILNKS QDYNLSENLS
PNLHNQGVML PYTGLHHLLF KYTLEPAYVM TSANMPGNPM LIDNKEILSK LDNIADYYLL
HDRKILNRCD DSVVRFRNGK PGFIRRSRGY VPKPFDFSKI NNTDNILAVG PELDVTFSIL
KEGKCYPSQH IGNTSKIRTL EFMQDAIKHL LKLTRTDSLN YIVADMHPEF NTTKLAKQLS
EEYDAQLVQV QHHHAHASSL MAEHQLPEMV VIAADGVGYG EDGNIWGGEI LYLNNTGHYI
NHGGLQTQPM PGGDLSTKYP IRMAMGILYG VMDSDELGKL MKSDYADYFK YGEQEVDMVL
KQLENDFNTS KTSSMGRVLD SISVLLGISK NRGYEGECSM KLESVAREGF DLLNIDLDFE
MIDDRAIINT SNLLLDVVQL IKSGVGADEI ACACQRALAE ALTEIAIIAA KSNKTSTIGV
TGGVFYNEFI SKVVKEKVIS AGFEFVQHEA TCAGDGSVSM GQCAIVGWRN SSLNELI
//
