ID L0F9S5_DESDL Unreviewed; 771 AA.
AC L0F9S5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=Desdi_2536 {ECO:0000313|EMBL:AGA69957.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA69957.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CP003344; AGA69957.1; -; Genomic_DNA.
DR RefSeq; WP_015262928.1; NC_019903.1.
DR AlphaFoldDB; L0F9S5; -.
DR STRING; 871963.Desdi_2536; -.
DR KEGG; ddl:Desdi_2536; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_9; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000010797; Chromosome.
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:UP000010797};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 4..88
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 193..380
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 771 AA; 85661 MW; E14AA787E9D8FAAE CRC64;
MKRAYSIHLN GIVQGVGFRP YVYRLALEMG IKGWVNNSSH GVGIHAEGLQ VDIFYTRLLS
ETPPVAKITQ AECEEAVFCY YETFEILQSE DDGLADVLIS PDIATCADCF SDLRDLKNRR
HNYPFTNCTN CGPRYTIIED VPYDRIQTTM KDFPMCEDCA HEYENPADRR FHAQPVACTQ
CGPTIQLLDA QGGALEGLGI MQIVQGAILA VKGLGGFHLV CDARDSAAIQ HLRQRKERGA
KPFALMARNL EVIRKFFRLS AQEEALLRSP AAPIVILERK KESKDYLPQE IAPGIHTLGV
MLPYTPLHAM LFDGPYDFLV MTSANLSGRP LIYRNEEALS ELGGIADYFL IHNRDIYHPC
DDSVLQVIGE ETVWHRRARG YVPLPQAGPK GQLTPILGVG GELKNAFCLA AEGRAFTSQY
IGDMEGYENF QRFRQEFTSF QKVVKIVPEV VAFDAHPNYQ TTRFAQEGPW LSKIKVQHHH
AHLVSVLGEH GITAPTLGVV CDGTGWGEDQ TIWGFEFLKG SSAGYERLAH LEYLPLPGGD
AGAKHPLRIA YAYGKTLLSP HEWAKTQELW EGLAASEQKI LDQQLEKRIN VFKTSSCGRL
FDAVSAVLGI CTKVTYEGQA AIELESKATT WLHNVWDISG SGASEELLGL SPRYPMEWDE
DEEGLVLRIK GIFARIMQDL LEGKENGFIA TYFHDSIAHG IVQTVLRLQA DQGPVALTGG
VFQNKLLTER VLELCKIHDI PVLRAKELPP GDGGLAYGQV IIANERCSSC V
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