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Database: UniProt
Entry: A0A225E9R3_9BACT
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ID   A0A225E9R3_9BACT        Unreviewed;       760 AA.
AC   A0A225E9R3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=FRUB_01646 {ECO:0000313|EMBL:OWK45315.1};
OS   Fimbriiglobus ruber.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Fimbriiglobus.
OX   NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK45315.1, ECO:0000313|Proteomes:UP000214646};
RN   [1] {ECO:0000313|Proteomes:UP000214646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA   Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA   Mardanov A.V., Dedysh S.N.;
RT   "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT   Planctomycetales with confirmed chitinolytic capability.";
RL   Submitted (JUN-2017) 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:OWK45315.1}.
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DR   EMBL; NIDE01000002; OWK45315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225E9R3; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000214646; 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   Reference proteome {ECO:0000313|Proteomes:UP000214646};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          3..89
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          198..383
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   760 AA;  81220 MW;  0D5A1B812CBD3C7C CRC64;
     MKRRAIIVRG LVQGVGFRPF VYGLARRLGL NGYVRNQTGG VWIEVEGEAE IIGRFLDGLT
     AEAPPAARIE DVSWESRTPV GDGDFRIEAS AADGGPVAIG PDLATCDACL AELFDPSDRR
     FHYPFLNCTQ CGPRLTIIIS APYDRERTTM AGFTMCPACR AEYDDPTDRR FHAQPVACPA
     CGPRLSLVDG DGSPRSVADP LGEAVAAVRA GQILAVKGLG GYHLACDAGN EGAVAELRRR
     KHRDEKPFAV MVADIEAAKR LAEVSDAEAT LLRDPRRPIV LLRRRPSAGL AAGVAPGNPA
     VGLMLPYTPL HHLLLRDAGG PLVMTSGNRS DEPIAFDDAD AITRLRGIAD QFLTHDRRIN
     IRADDSVTRW SAGAEAPVRL SRGYAPGTVS LACECPEPTL AVGGQLKSVF ALGRGRQATL
     GHHLGDLDHA EAFRAFTAAV AYYEQLFGFK PAVLVHDLHP DYASTRYALE RDDVPRRIAV
     QHHHAHLASC LAENGLDEPA IGVTFDGSGY GLDGTIWGGE FLVGDCGSVR RAAHLRAVPM
     PGGEQAVREP WRMALAYLVD AGVEPAILSP AVPTVSLRTA RQLLTKRALA PLTSSAGRLF
     DAVAAIAGVR HRVSYEGQAA IELEGLAATA APDESYPFEV TAGAEAWEID CRPLVAAVER
     DAARGEFAAR IARRFHTTLV EIIARTCDRL RVESGLSLVA LSGGVFHNGL LLGETVARLQ
     ADGFRVCRHR RVPAGDGGLC LGQLAVAAAV ATRTEQKLCA
//
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