ID K4L3B1_9FIRM Unreviewed; 826 AA.
AC K4L3B1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=DCF50_p929 {ECO:0000313|EMBL:AFV04934.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV04934.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV04934.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV04934.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
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DR EMBL; CP003870; AFV04934.1; -; Genomic_DNA.
DR RefSeq; WP_015042937.1; NC_018867.1.
DR AlphaFoldDB; K4L3B1; -.
DR STRING; 1131462.DCF50_p929; -.
DR KEGG; dec:DCF50_p929; -.
DR PATRIC; fig|1131462.4.peg.938; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_9; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000000482; Chromosome.
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; 1.10.357.160; -; 1.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 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; 2.
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:UP000000482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 4..88
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 195..382
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 19
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 826 AA; 92295 MW; ED561CE7530CE101 CRC64;
MTRAVRIRIN GIVQGVGFRP FIFKLARELD IKGWVNNFSG GVEIQAEGER VEDFIRRIRT
DRPTLAVIVS LEITEIPVQH YREFTITESR ESEDKDVLIS PDVAVCRDCL QEMLHSKDRR
YLYPFINCTN CGPRYTIIKD QPYDRKKTTM AGFQMCPECH QEYLDPLDRR FHAQPTACAV
CGPALKLLDR TGNEISGNGI GIDLLQEGAI LAVKGLGGFH LVCDACNHEA VSRLRRVKER
GAKPFAVMAR NIETALKEVT ITELEKSTLA GPSAPIVLLP RKKNENSRIS PKTAPGLQSL
GIMLPYTPVH HLLFQGTYDY LVMTSANLSG QPLIYDNQEA LAGLSGIADY FLLNNRDIYH
PCDDSVMQMI GDQMTFIRRA RGYVPLPLFL KQEIKTPIVG LGGEMKNAFC LASGKMAFMS
QYIGDMHGYE NLERFEQELY SFQKVTNIAP QKTAYDMHPE YSTTRIARSM DRPKIRIQHH
HAHLVSVMAE HGMDEPMLGL ICDGTGYGED GRIWGFEYLF GNQEGYERKA YLEYLPLPGG
DAGAKYPLRI AYAYLKKLMT QEEWQRTEPL WTKLSSQEKN ILDGQLRSGF QLFETSSAGR
LFDAVSGMLG VCTEVTYEGQ AAIELESVAE KWLEDGNKDI QKNLNEFQKI RLQASMRVKA
SAALLDQHGI SGQTIAEKRL KLIEQYNEIA GKTDGSFCPG LYPALYPACL EISGEPQPGV
LHVKVGSLLK EIANDVLLQK NPGEAALRFH YSLACQMLET AMLIGLENKK LPIAGGVFQN
KLLTEILMFL AEGIGVEILY PQKLPSGDGG LAFGQVLIAN AVNQKC
//
