ID Q3AT69_CHLCH Unreviewed; 749 AA.
AC Q3AT69;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=Cag_0533 {ECO:0000313|EMBL:ABB27806.1};
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB27806.1};
RN [1] {ECO:0000313|EMBL:ABB27806.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB27806.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) 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; CP000108; ABB27806.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AT69; -.
DR STRING; 340177.Cag_0533; -.
DR KEGG; cch:Cag_0533; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_10; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 199..384
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 749 AA; 82326 MW; 27E8CFCA777E2F84 CRC64;
MQRQRLLING IVQGVGFRPF VYRLAIEHEL TGFIRNTALG VLIEVQGSAD RLDSFCTALH
HQPPPLARIA SFEMHFIPCV FEEATFVITD SHSGGDVETL IPPDIALCSD CRRELYDPTN
RRYRYPFINC TNCGPRYTIV AHLPYDRPTT SMQSFAICPE CEQEYHNPLD RRFHAEPTCC
PICGPSLSLL DADGNAIADD PLEETASLLH HGAIVAIKGI GGFHVAVDAL NDDAVLRLRK
SKGREAKPFA VMMRDVAVVE RYCMVNDDER QALLSAEAPI VLLKKLANTQ LAASVAPDND
RLGVMLPYTP LHLLLFDRVP EVLVMTSANM SEEPMVHENS EALQKLQGIA DAFLMHNRPI
YLKCDDSVTI HLAGQLRQLR RSRGYVPAPL LLRHSGATLL ATGGELKNSV TLLKAHHAIM
SQHIGDVKNF DAYCHFEQVV AHLQHLFQAT PELIVHDLHP AYLTTQWAEK QAIPTLGVQH
HHAHLAACLA ENQVDEPAIG VILDGTGYGT DGTVWGGEVL IGDVANFERF ASLELMPLAG
GEAAIRQPWR AAVGYIYKSC GSLPDLPFLQ NRDIAPIMEL LERQLHLVET SSCGRLFDVV
AALCNLRGTI TYEGEAAIAL MHAANGTVGR QPFPYDLCYQ LNRWIIGIAP MIRSIVNSLL
HGASAQEVSQ RFHGTLVHCF CEVVQKASEA TGLKIVALSG GVFQNELLFT ALVHALEQAG
FTVLTHSRVP TNDGGLSLGQ AIIGRRFLA
//
