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Database: UniProt
Entry: A0A0P6XGV1_9CHLR
LinkDB: A0A0P6XGV1_9CHLR
Original site: A0A0P6XGV1_9CHLR 
ID   A0A0P6XGV1_9CHLR        Unreviewed;       770 AA.
AC   A0A0P6XGV1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=SE15_11745 {ECO:0000313|EMBL:KPL82733.1};
OS   Thermanaerothrix daxensis.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Thermanaerothrix.
OX   NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL82733.1, ECO:0000313|Proteomes:UP000050544};
RN   [1] {ECO:0000313|EMBL:KPL82733.1, ECO:0000313|Proteomes:UP000050544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GNS-1 {ECO:0000313|EMBL:KPL82733.1,
RC   ECO:0000313|Proteomes:UP000050544};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL   Submitted (JUL-2015) 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:KPL82733.1}.
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DR   EMBL; LGKO01000005; KPL82733.1; -; Genomic_DNA.
DR   RefSeq; WP_054522279.1; NZ_LGKO01000005.1.
DR   AlphaFoldDB; A0A0P6XGV1; -.
DR   STRING; 869279.SE15_11745; -.
DR   PATRIC; fig|869279.4.peg.1970; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000050544; 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   Reference proteome {ECO:0000313|Proteomes:UP000050544};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          7..93
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          204..392
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   770 AA;  86240 MW;  181F3F898C95A8A8 CRC64;
     MKPSSQGLYI RIRGIVQGVG FRPFVYTLAT RHHLNGWVRN TAAGVEIEVC GDPRALQSFV
     ADLQTQAPPL ARIDSFEVFP SSTNHWTSFQ IIESQANAEE FLPVSPDVAI CPECRQELFD
     PKNRRYRYPF INCTNCGPRF TIIRTIPYDR PNTTMAEFPL CPACSAEYHD PTNRRFHAQP
     IACPECGPHL QFLTPEGKVV AEREAALQLA RTWLAEGRIL AIKGLGGYHL ACDATRPESV
     RELRRRKQRS DKPFALMAFD LSIIARHARV SESEQNLLTA PQHPIVLLER IPTSLIASEV
     APGQRTLGFM LPYTPLHLLL LEPAPGFPEA LVMTSGNLSE EPIAYRDKEA LERLSRLADG
     FLIHNRPIHT RVDDSVIRSF NHRPYPLRRA RGYAPDPIRL PQEVPPILAT GGELKNTFCL
     TRGTYAFLSH HIGDLQNYET FQAFEEGIQH YERLFRTRPE WIVADLHPDY LATHYAQERA
     RAENIPLLLV QHHHAHLAAC LADNGIKDPE PVIGLIFDGT GYGTDGSIWG GEVLIGTYGG
     YHRYAHLTPV PLPGGDRAVH QVARMALAHL WACKLPWDED LPPVKALCPE ERTLLRSMLE
     RKINSPLTSS MGRLFDAVAA LIGIRAEANY EAQAAMELES LVDEDEKGVY PLPVEPPTIL
     LRPFWEAILD DLRRGTPSPR IAARFHNSIV NLCVDVAEQI RQAKGLNRVV LSGGVWQNQV
     LLRHTMRALE QKGFQVFIHL QVPPNDGGLA LGQAMIGASW IKVNPHSTGF
//
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