ID B3EL94_CHLPB Unreviewed; 767 AA.
AC B3EL94;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN OrderedLocusNames=Cphamn1_1764 {ECO:0000313|EMBL:ACE04682.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE04682.1};
RN [1] {ECO:0000313|EMBL:ACE04682.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE04682.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-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; CP001101; ACE04682.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EL94; -.
DR STRING; 331678.Cphamn1_1764; -.
DR KEGG; cpb:Cphamn1_1764; -.
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; IPR043129; ATPase_NBD.
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; SSF53067; Actin-like ATPase domain; 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 12..99
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 209..394
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 27
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 767 AA; 84148 MW; 3DC175D722B00D07 CRC64;
MDRMAAVKTE KRVRCFVSGI VQGVGFRPFI YRLAKGAGLS GYIRNTSSGV CIEIQSPESS
KLDRFFFDLR HMAPPLAKIT SIEIEEIPPS SEREFVIMSS DDEGAAETLV APDIAMCEAC
RKELLSPSDR RHGYAFLNCT DCGPRYTIIE RIPYDRRYTS MKDFTMCPDC EREYHDPMDR
RFHAQPNACP VCGPSLQILD RDGNVVPCDD PVGYAVASLK SSGVVAVKGI GGFHLSVDAF
DDKAVSALRK RKRREEKPFA VMARSIETIE KFCDINASER EALCSPQAPV VLLKKKARHG
LSEEIAPRND RLGVMLPYAP LHVLLMNRGP EMLVMTSANS SDEPIAIENS EAVSRLQEIA
DCYLVHDRPV YLRCDDSVTV HLAGKLRQVR RSRGYVPEPV PLLSGGASVF STGAEIKNTV
CLLKGNSAIV SQHIGDLRNY ESYRHFQMVA DHLQQIFQAS PELIVSDMHP AYLSSLWALE
QKDIPSLAVQ HHHAHLASCL AENLSDAPAI GVILDGTGYG IDGTSWGGEV LIGDAAEAYR
FACFDPVPLP GGDAAVFHPW RAAAGYLFHS FDTVPEPGFM RDKDMSGVMQ LLEKGVNSPV
TSSCGRLFDA VAALTGLCSD ISYEGQAAIE LMLAARGFEG EPFSWEISAS GDDRWRLDIS
PMIRDIVTAV QSGVPVAVIS SRFHVTIVEL LYAIVRKAVA YSGIHRVVLS GGVFQNALLF
ERLTEKLERH GLTVLTHALV PCNDGGISLG QAVIGREYLK GRYKGVL
//
