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Database: UniProt
Entry: B5JEL9_9BACT
LinkDB: B5JEL9_9BACT
Original site: B5JEL9_9BACT 
ID   B5JEL9_9BACT            Unreviewed;       774 AA.
AC   B5JEL9;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=VDG1235_347 {ECO:0000313|EMBL:EDY80730.1};
OS   Verrucomicrobiae bacterium DG1235.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY80730.1, ECO:0000313|Proteomes:UP000003839};
RN   [1] {ECO:0000313|EMBL:EDY80730.1, ECO:0000313|Proteomes:UP000003839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG1235 {ECO:0000313|EMBL:EDY80730.1,
RC   ECO:0000313|Proteomes:UP000003839};
RA   Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS990592; EDY80730.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JEL9; -.
DR   STRING; 382464.VDG1235_347; -.
DR   eggNOG; COG0068; Bacteria.
DR   HOGENOM; CLU_009164_0_0_0; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000003839; 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:UP000003839};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          14..100
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          211..394
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   774 AA;  85779 MW;  B2153758D2CA1832 CRC64;
     MPVFTNNRQA KHKRLQVFIH GAVQGVGFRP HVYRLARDLN LVGWVINNSQ GVRIEVEGLA
     FDLEQFLDRL KSEKPPLAQV TSIESRYVKP VGFSDFRVRH SDSNGEKTAL ILPDIATCPE
     CQAELFDPKD RRYRYPFINC TNCGPRFSIV ETLPYDRPNT TMKRFPLCPL CQKEYDAPEH
     RRFHAQPIAC STCGPTLEFW NKATGPCAHG DEALKMAEHL VSSGHVLALK GVGGFQLIVD
     ARNADAIARL RKCKGRGPKP LAIMCPDLGY TRSICHLSAL ERKLLLSPAS PIVLLKKRSR
     AFDAVAPGMR DYGVMLPCSP LHHLLMRDLG YPIVATSGNR SEEPICIENE EAIERLSDIA
     DAFLMHDRPI ARHVDDSIAR VILGDVQILR RARGYAPLPI NVDLEIPSCI ALGAHLKNSV
     AIVAQNKIFI SQHIGNLETA ESYRAFETTA RDLPILYDCQ PTFVAHDKHP DYVSTFYARG
     TPLERISVQH HLAHVYSCMA DNQLQAPVLG ISWDGTGYGD DKSVWGGESF LIEDSAERRV
     SSITQFPLLG GDIAALQPRR VALALLQASF PKSLGDYAKL PALRAFTASE YRILEQITLK
     HRNPLTSSIG RLFDGVSSIL GICQTNRFEG QAAALLEFLA ATAPKNQLPY PYILHDQGGF
     TTFDWKPMIR AIVEEYTNGV NPPIIAARFH QTLAAYAVDI ASRHGVPSIA LTGGCMQNRL
     LCELIAETLK ENGFNPFIHR RVPPNDGGIC VGQAYAVGRT HQTSPSLQHE TPCV
//
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