ID A0A0S4L7I1_9BACT Unreviewed; 797 AA.
AC A0A0S4L7I1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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 Name=hypF {ECO:0000313|EMBL:CUS32730.1};
GN ORFNames=COMA1_10783 {ECO:0000313|EMBL:CUS32730.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS32730.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS32730.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS32730.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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; CZQA01000001; CUS32730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4L7I1; -.
DR STRING; 1742972.COMA1_10783; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000199032; 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:UP000199032};
KW Transferase {ECO:0000313|EMBL:CUS32730.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 8..94
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 205..409
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 797 AA; 86970 MW; F2D2B07D1A46D50E CRC64;
MRKTLAQRVQ VNVRGTVQGV GFRPCVYRLA RELELTGWVR NSRNGVVIEV EGTAEAIETF
LERLQADAPA AASIEAISTS LIPARGDASF TIVTSAESGE RTLVIPPDLA TCVDCLLELA
DPQDRRFRYP FLTCTQCGPR YSLLTAIPYE RSNTTMAGFE LCSDCRAEYE TDTGRRFHAE
PIACSDCGPH PSLWDEQGQE TARGEEALQQ AVALLRQGLI VAVKGLGGFQ LWVDAESEKA
VQRLRDRKRR LEKPFAVLFS SVDAVKDYCV LSSHEASLLC SPQAPILLAR KRQDTAIAEA
VAPGNPYLGV MVPTTPLHHL LMASLQRPMV ATSGNRSEEP IVIDEHEALI RLKGIADALL
VHDRPIARPV DDSVVLVVER MPEHHERGEE RSEADQRKND RLILRRARGY VPQAICWRDD
SSDKNGQGPI LAVGGHLKNT VALLTGHRVV LSQHLGDLST VEADQAFRQA IEDLQRLLQI
EPQAIACDLH PDYRSTSFAR QLAASLTVPL IPVQHHHAHV ASCMAEHKLD GEVLGIAWDG
AGYGGNGQVW GGEFLVASYL GFSRFASLKP FRLPGGEAAM RDPNRSAAAV LWELMGEEML
GHDLPSWEDT SDRCRQLAIL LRSGIASPWT TSLGRLFDAV ASLTGLCSQA SFEGQAAMAV
QFAAEREWEA SGGRVQSYPI DLLRSANSDT KWMVDWLPMI SAMLDDLHRG CRLEKIAAQF
HVSLADATVR VAHAAGLPRV VLTGGCFQNR LLLSLVRGRL EKAGFTVYSH SLVPPNDGGL
SLGQAVVAAC SKGTVSG
//
