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Entry: A0A1G9Q0G9_9ACTN
LinkDB: A0A1G9Q0G9_9ACTN
Original site: A0A1G9Q0G9_9ACTN 
ID   A0A1G9Q0G9_9ACTN        Unreviewed;       819 AA.
AC   A0A1G9Q0G9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=SAMN05444921_103203 {ECO:0000313|EMBL:SDM04496.1};
OS   Streptomyces wuyuanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM04496.1, ECO:0000313|Proteomes:UP000199063};
RN   [1] {ECO:0000313|Proteomes:UP000199063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
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; FNHI01000003; SDM04496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9Q0G9; -.
DR   STRING; 1196353.SAMN05444921_103203; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000199063; 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-KW.
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   Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          23..109
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          238..437
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   819 AA;  86206 MW;  4FDD62B9BC83873A CRC64;
     MTTSAPGPAA SRPGPVAPAS VQRRRVTVRG VVQGVGFRPF LHNLATGLHL TGHVTNTGDG
     VVAEVEGAPV AVARFCARIA DEAPPLALVE SVHDQEVPVA GDSGFLIVAS DKGGPVRTLV
     SPDTATCADC LRELADPGDR RHRHPFITCT HCGPRFTIVT GLPYDREHTT MADFPMCPDC
     AREYSDPGDR RFHAQPVACP SCGPRLRMIV APAAPGLRPR HVVAPDPNDR SLGGPVVADP
     VREARELLSD GAILAVKGLG GYHLACDAAN KGAVALLRRR KARGDKPFAL MAREIGDIEH
     LVHLGAAERE LLTGAVRPIV LMRRRTTPLE APPGAPRPVD GVAPGSPDLG VMLPYTPVHQ
     LLLGLPGEEH AGPRLLVMTS GNLAGEPIVT DDGEALERLA DLADAWLLHD RPIHVPCDDS
     VVRVCDGELL TLRRSRGHAP LPVTLPLPVP PALAVGGDLK NTFCLGRDRK AWLSAHIGDM
     DDLATQHAFA CAEEQLEEIT GVRPELLAVD RHPGYRSARW ARHNAGERPV VRVQHHHAHI
     ASTMAEHGLD GSRPVIGVAF DGTGYGDDGA VWGGEILLAD YDGFHRCAHL GYVPLPGGDS
     AVQRPYRMAL AHLHAAGIGW SGDLPCTAAC PEQELPLLRK QLERNLNCVP TSSMGRLFDA
     VSSLAGVCHL ARYEAQAAIE LEAAAVRADG AYGQPYSFGL LPAGGGPAAS MTADPEPVLA
     AVVEDVRAGV PAPVIAGRFH ASVAALVRRV CALARERHGL ETVALTGGVF ANAVLSSACA
     AGLREDGFTV LRHHRIPPND GGLALGQLVV AARAAGGTG
//
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