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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//