ID T2IIF0_CROWT Unreviewed; 768 AA.
AC T2IIF0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=CWATWH8502_3055 {ECO:0000313|EMBL:CCQ52612.1};
OS Crocosphaera watsonii WH 8502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423474 {ECO:0000313|EMBL:CCQ52612.1, ECO:0000313|Proteomes:UP000018348};
RN [1] {ECO:0000313|EMBL:CCQ52612.1, ECO:0000313|Proteomes:UP000018348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8502 {ECO:0000313|EMBL:CCQ52612.1,
RC ECO:0000313|Proteomes:UP000018348};
RA Bench S.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCQ52612.1, ECO:0000313|Proteomes:UP000018348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8502 {ECO:0000313|EMBL:CCQ52612.1,
RC ECO:0000313|Proteomes:UP000018348};
RA Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT "Whole genome comparison of six Crocosphaera watsonii strains with
RT differing phenotypes.";
RL Submitted (SEP-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ52612.1}.
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DR EMBL; CAQK01000687; CCQ52612.1; -; Genomic_DNA.
DR RefSeq; WP_021831490.1; NZ_CAQK01000687.1.
DR AlphaFoldDB; T2IIF0; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000018348; 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; 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 6..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 202..390
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 768 AA; 86376 MW; 7427AF88CD45C6BE CRC64;
MNQFNRLKII IQGAVQGVGF RPFIYRLARE LNLKGWVNNS AAGVFIEVEG SETNLKKFLS
RIDKEKPPIS QINSLETTWL EPVNYTNFEI RHSSGGEKTA IVLPDLATCP DCLQEIFDPH
NRRYLYPFTN CTNCGPRYTI IEELPYDRPH TTMKNFTMCE SCQAEYENPL DRRFHAQPNA
CPVCGPRLQL WDKKGEILGN DNDALNLSIN ALKKGQIIAL KGLGGFQLIV NAKNRESVQQ
LRKRKHRPHK PFALMDSSLE NIKSYCEVND IEAQLLSSPQ APIVLLKRKS KTPLDDLSPN
IAPNNPYLGV MLPSSPLHHL LLHKIDFPLV ATSGNIASEP ICIDEKEALK RLENIADLFL
VHNRPILRPV DDSVVRVIAG REMIIRRARG YAPFPITINT QQKDNNYPNI LAVGGHLKNT
VAILKNNQVF ISQHIGDLST AEALKSFNQV MESLKGLYDF EPEIIVCDAH PDYVSSQYAK
SQNLPVITVQ HHYAHLLSCL ANTPLLNTNC NLDAPVLGIT WDGTGYGNDN TIWGGEFLLV
DNNQYERIAH FRTFKLPGGD QAVKDPRRIA ISILFEVLGD NNSLKLPFLE TVSSKELNLI
KQMLARNLNT PLTSSVGRLF DAVAAMIGIC ENISFEGQGA MALEYAINDL KTDEIYPYQI
TGLTYPFVIN WQLIIESIIE DILQKTSHQE IAAKFHNTLV EIIIDIAQKS QQKNIILTGG
CFQNKYLSER TIFRLKQEKL TPFWHHNIPP NDGGIALGQI IAGILEKK
//
