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Entry: A0A165Y3S0_9BACI
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ID   A0A165Y3S0_9BACI        Unreviewed;       753 AA.
AC   A0A165Y3S0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=AZI98_07290 {ECO:0000313|EMBL:KZN96700.1};
OS   Aeribacillus pallidus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX   NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN96700.1, ECO:0000313|Proteomes:UP000076476};
RN   [1] {ECO:0000313|EMBL:KZN96700.1, ECO:0000313|Proteomes:UP000076476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8m3 {ECO:0000313|EMBL:KZN96700.1,
RC   ECO:0000313|Proteomes:UP000076476};
RA   Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., Korshunova A.V.,
RA   Sokolova D.S.;
RT   "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT   reservoir.";
RL   Submitted (APR-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|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}.
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:KZN96700.1}.
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DR   EMBL; LWBR01000016; KZN96700.1; -; Genomic_DNA.
DR   RefSeq; WP_063387620.1; NZ_LWBR01000016.1.
DR   AlphaFoldDB; A0A165Y3S0; -.
DR   STRING; 33936.AZI98_07290; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000076476; 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:UP000076476};
KW   Transferase {ECO:0000313|EMBL:KZN96700.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          4..90
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          200..383
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   753 AA;  83665 MW;  33119AC8511BC77F CRC64;
     MKIAQRIRIY GVVQGVGFRP FVFRKAKRWK LRGWVRNGES GVEIHVEGDA DAIQQFVQEI
     TDRYPSSAKI TNLEIKDAPL QEAADFKILA STLHNRPTVQ IPADLAVCPK CLSELFDPAN
     RRFLYPYINC TDCGPRYTVI ERLPYDRPYT TMHMWSMCPA CSAEYYDPAD RRFHAQPTAC
     PDCGPHYHVQ GQDGEIHGDE KAIKKTAELL RSGLIVAIKG LGGYLLACDA ENEEAIWELR
     RRKRRGEKPF ALMVKDLETA RAFIDICAEE ENFLTSSARP IVLARARRLL PGVAPDNSDL
     GVMLPYTPLH HLLFHFDAPE VLVMTSANRS SEPIIYDDEE ALKALEGIAD AWLIGERPIA
     RRVDDSVVRV SPFGPTVLRR ARGYAPLPAA QLPSDRPVLA VGADLKNTIT LVVNGQAIMS
     QHLGDLIKYE AYMSFEQTVH DLLSMYDVRL QETIVAYDLH PDYQSTTFAH NLEAYQHIGI
     QHHRAHVASV LAERNALDKR VIGVAFDGTG FGDDGAIWGG ELFVGSAAEG LKRRGHLRYA
     MLPGGDAAAR MPLQALAGFF VDDPKWAINV GKQLSFPERF FTAVKMVEKQ LRTFPTTSVG
     RLFDAAAALL GFTGPISFEG QAAIWLEHLA RTAPLEKVYS FPWNGKELDY RPFLKEMTED
     RLKGKDAAVI ARAFHRSVAE GIFRSVRSLG AAYEIDTVVL SGGVFQNSLL LADLKELFFE
     SDMHIWVGEE VPPNDGGISL GQAALAAAAH SNL
//
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