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Database: UniProt
Entry: A0A1Q3TKE0_9CHLR
LinkDB: A0A1Q3TKE0_9CHLR
Original site: A0A1Q3TKE0_9CHLR 
ID   A0A1Q3TKE0_9CHLR        Unreviewed;       771 AA.
AC   A0A1Q3TKE0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=BGO39_05925 {ECO:0000313|EMBL:OJW02763.1};
OS   Chloroflexi bacterium 54-19.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJW02763.1, ECO:0000313|Proteomes:UP000186384};
RN   [1] {ECO:0000313|EMBL:OJW02763.1, ECO:0000313|Proteomes:UP000186384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54-19 {ECO:0000313|EMBL:OJW02763.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW02763.1}.
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DR   EMBL; MKTJ01000017; OJW02763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3TKE0; -.
DR   STRING; 1895928.BGO39_05925; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000186384; 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; 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   Transferase {ECO:0000313|EMBL:OJW02763.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          11..97
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          207..400
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   771 AA;  84422 MW;  43F14D821790E52D CRC64;
     MANLTETTMQ RQRLLVQGLV QGVGFRPFIY GLALRLDLGG FVLNDSEGVT IEIEGSPEQL
     VAFHSALHDE LPPLARVDSL VTALIPTHHE SAFRIVHSQA GGEKHALISP DSATCPDCLH
     ELFDPHDRRY RYPFINCTNC GPRFTIVKDV PYDRDQTTMA VFPMCPACRV EYEDPLNRRF
     HAQPNACPVC GPQVRLLAQD GQPLEVADPI EAAARQLAGG AILAIKGLGG YHLACDALDE
     AAVARLRSRK HREAKPFALM VPDLAVARQL CELNEAEEKL LQARQRPVVL LLQRPGAGLA
     PAVAPNYHTL GLMLPYTPLH YLLLDAFKRV VGLDRPAALV MTSGNMSDEP IAYRDGDATT
     RLAPVADGWL THNREIHMRC DDSVVRVLDG SPQFFRRSRG YAPEPLRLNR TFARPVLACG
     GHLKNTFCLA KERQAFVSHH IGDLENLETL TSFREGIAHY ERLFDITPQV VAYDLHPDYL
     ATRYALDLDL PHKIGVQHHH AHIASVLAEH GLTGPVIGVA ADGTGYGGDG TIWGCEIMLA
     SLLKFERLAH LAYIPLPGGD RAVRQPWRVA ASLLTQVYGE NFLDLEIPFA RQLDPARWKP
     LAQMITRGVN SPLASSLGRL FDGVSALVGL RQEVVYEGQA AIELEALALP ADRPYPFSIK
     EGQPAILDVG PLLRAIVDDL KEGVPAGLIA GRFHRSIAEL LAAVCRLARA QTGLNEVALS
     GGVFQNRLLL EQLLGLLEEA HFTVYRNCQV PPNDGGLSLG QAVVAAARLE T
//
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