ID Q8GGQ6_STRAZ Unreviewed; 791 AA.
AC Q8GGQ6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
OS Streptomyces atroolivaceus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66869 {ECO:0000313|EMBL:AAN85509.1};
RN [1] {ECO:0000313|EMBL:AAN85509.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12446651; DOI=10.1128/JB.184.24.7013-7024.2002;
RA Cheng Y.Q., Tang G.L., Shen B.;
RT "Identification and localization of the gene cluster encoding biosynthesis
RT of the antitumor macrolactam leinamycin in Streptomyces atroolivaceus S-
RT 140.";
RL J. Bacteriol. 184:7013-7024(2002).
RN [2] {ECO:0000313|EMBL:AAN85509.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheng Y.-Q., Tang G.-L., Shen B.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAN85509.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12598647; DOI=10.1073/pnas.0537286100;
RA Cheng Y.Q., Tang G.L., Shen B.;
RT "Type I polyketide synthase requiring a discrete acyltransferase for
RT polyketide biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3149-3154(2003).
RN [4] {ECO:0000313|EMBL:AAN85509.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15112993; DOI=10.1016/S1074-5521(03)00286-2;
RA Tang G.L., Cheng Y.Q., Shen B.;
RT "Leinamycin biosynthesis revealing unprecedented architectural complexity
RT for a hybrid polyketide synthase and nonribosomal peptide synthetase.";
RL Chem. Biol. 11:33-45(2004).
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; AF484556; AAN85509.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GGQ6; -.
DR UniPathway; UPA00335; -.
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; 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; 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 6..96
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 206..397
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT REGION 771..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 791 AA; 85473 MW; 9536FC0FDDFD725E CRC64;
MAETEQWLIR VTGVVQGVGY RPFVHTLATG LGLRGWVLND TLGVQTEVSG GAGELAEFAG
ALKDRAPLLA RVEEVRVESR TPRAGGDLPT GFEIRESRRT GRANTIVAPD SHVCDDCLRE
VLDPTDRRFR YPFTNCTHCG PRYSLIKGLP YDREKTTMAV FAMCEDCRAE YVNPADRRYH
AQPTACPRCG PKVALSAPDG VVAEADEALT RTIRALGDGQ IVAVKSVGGF HLAVNARDAA
AVARLRRRKK RDSKPFAVMA AGLDETAAIA HITDAERELL RSPARPIVLL RKLPGALPEE
VAPRNPNLGV MLPSAPLHQL LLDRPESDVL VMTSGNISGQ PIAYRNEDAL AELFEVADLI
LHHDRDIHVR VDDSVVRSSV HPALDEPIIT FLRRSRGYAP YPVKVDDIAG PVIAYGAELK
TTVALGDGNE VYVSQHIGDL KNDETYASHR EAAAHLAELY ELKPRHAACD LHPAFKARVL
AGTDRPDDVV EVQHHHAHMA SCMAENRLSG PTIGVVFDGA GYGEDGTIWG GEFLVGDFAS
VRRAAHLRPV PLLGGDKAVA EPVRTGYALA LQALGSPERA VAAFPALEIL DDRKRTVFAT
MAERGIQAPP VSSMGRLFDA VAALLGVCAY AEYEAHGPIE LEGLLGRDLA LTAPYAFGLQ
QEGDTELVDP RPLVRAIAAD LARGTGVTDI SRRFHSTVVD MVVKRCSALR ERTGIRQVVL
SGGVFLNEFL QVNCLVELRR AGFDAHAHRL VPTNDGGIAL GQVMVANARL RASPDSTDSP
ATPNPGTNEC R
//
