ID A0A1G4W485_9MYCO Unreviewed; 764 AA.
AC A0A1G4W485;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=SAMN02799620_02139 {ECO:0000313|EMBL:SCX15728.1};
OS Mycolicibacterium fluoranthenivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX15728.1, ECO:0000313|Proteomes:UP000199707};
RN [1] {ECO:0000313|Proteomes:UP000199707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FMUB01000004; SCX15728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4W485; -.
DR STRING; 1502745.SAMN02799620_02139; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000199707; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 205..395
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 24
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 764 AA; 80802 MW; CCAAFCB7BAF90EEF CRC64;
MTTTDRRRRL NIQVHGVVQG VGFRPFVYTT AAALGLAGSV RNDSSGAIIE IEGDAADVAG
FLTMLQDRPP PLAVIDAVQT QDLPPRGGTG FAIADTTHSG GGRTLASPDV AICDDCVAEQ
RDPTDRRYRH AFVNCTNCGP RFTITASLPY DRAATTMAAF PMCGACAREY ADPADRRFHA
QPICCPDCGP MPAFQDHDGH RTLGEDGLAR ARDLLRRGGI LAVKGIGGYH LACDAADSAA
VTELRIRKRR GDKPFAVMVA DLATAHTIAE VNLPAERVLT GPQRPIVLLP RRPGGPVDRA
VAPHLPDLGV LLAYTPLHLL LFGLPGDEPG PTALVMTSGN LGGEPICFTD HDAVDRLGPL
ADGWLLHDRA ILAPCDDSVV RVCARRQIPI RRSRGYAPLP VALPAPVPPT LAVGTDLKNT
MAVAAGKYAW LSQHIGDMDD LATLSAFDSA RHHLQALTGV TPEILVADAH PGYRSTAWAR
RNAAGRPVRS VQHHHAHIAA VMAEHGLDGA QPVLGFAFDG TGYGPNGAIW GGEVLLADYK
CYRRLAQLKY VPLPGGDISV LRPYRMALAH LWAAGLPWDD DLAPVRACPD EERRVLAHQL
QTGLGCVPTS SMGRLFDAVS ALAGVRQVVA YEAQAAIELE GHSRDRCCGA TSYAFPIEEG
DPAVIDPGPV LAAVVTDARL GVPTGVIGAR FHRAVADLII ELARTAARGA PVVALSGGVF
QNALLLGLAV DGLEARGVEV LTHHRVPPND GGIALGQLLV GNSS
//
