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Database: UniProt
Entry: A0A1A0M8B0_9MYCO
LinkDB: A0A1A0M8B0_9MYCO
Original site: A0A1A0M8B0_9MYCO 
ID   A0A1A0M8B0_9MYCO        Unreviewed;       789 AA.
AC   A0A1A0M8B0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=A9W99_13440 {ECO:0000313|EMBL:OBA81719.1};
OS   Mycobacterium sp. 1164966.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA81719.1, ECO:0000313|Proteomes:UP000092060};
RN   [1] {ECO:0000313|Proteomes:UP000092060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-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:OBA81719.1}.
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DR   EMBL; LZSG01000032; OBA81719.1; -; Genomic_DNA.
DR   RefSeq; WP_067376694.1; NZ_LZSG01000032.1.
DR   AlphaFoldDB; A0A1A0M8B0; -.
DR   STRING; 1856861.A9W99_13440; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000092060; 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; IPR043129; ATPase_NBD.
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; SSF53067; Actin-like ATPase domain; 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:UP000092060};
KW   Transferase {ECO:0000313|EMBL:OBA81719.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          17..105
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          215..412
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        32
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   789 AA;  84214 MW;  336D47304DDAFF0D CRC64;
     MTDTPVLALV SEPADVRQRF TVTGVVQGVG FRPFVHRIAT ELGLAGFVGN DSGAVFLEVQ
     GHHARVGEFA QRLRAQAPPL ARISAVSVVD VAPETGCGKQ FRIVASRTAA GAGTPIPPDV
     AACDECVAEL FDPNDRRYRH PFVTCTNCGP RFTIIGALPY DRRATTMSGF AMCERCAAEY
     HDPADRRFHA QPIACPDCGP SLWFSSAHGR IDRADAALAA TQRALGTGAV VAIKGIGGYH
     LACAVDDEAA VSALRARKAR GAKPFAILVR DLDVARRYAF VDGNEAAVLR GAARPIVLLR
     RRSGAPVAPA VAPGSPLLGL MLPYSPIHHL LLAPIPGTDA PVPDALVLTS ANRSDEPICF
     TDDDAAQRLP ALCDAVLNHD RPIHVPCDDS VVRVLSCASR RGGELPIRRS RGYAPLPVDL
     GITGPAVLAV GGELKNTFCL TDGSRAYLSG HIGDMGTWET LRAFERAVRQ LSELRCSPVR
     VAADLHPGYH TRSWAERHAG GRPLDLVQHH HAHVVSLLAE HGRIGEPVIG VAFDGTGYGC
     DQTIWGGEIL RLGHDSHRFV RAGHLLPVPL PGGDAAVRNP WRMALSQLWM AGIDWTPRLP
     PVAAATPDEL RLIRSQLESM TGCVPCSSMG RLFDAVASLL GVRHRIDYEG QAAIELETLA
     DSVHDSARPM PSLSLTVRPD NVIDPAAMMQ ELVSALNAGE QPAPLAAAFH RAVADAVATV
     VRQVAGTVRA VGLTGGVFQN VLLLRECRER LQRNGFEVLT HQLVPPNDGG LSLGQAAISM
     LTAREEADR
//
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