ID A0A1V3TQT9_9PAST Unreviewed; 761 AA.
AC A0A1V3TQT9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=BMT54_08280 {ECO:0000313|EMBL:OOH88809.1};
OS Pasteurellaceae bacterium 15-036681.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae.
OX NCBI_TaxID=1924934 {ECO:0000313|EMBL:OOH88809.1, ECO:0000313|Proteomes:UP000188845};
RN [1] {ECO:0000313|EMBL:OOH88809.1, ECO:0000313|Proteomes:UP000188845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15-036681 {ECO:0000313|EMBL:OOH88809.1,
RC ECO:0000313|Proteomes:UP000188845};
RA Stuber T.P., Hicks J.A., Robbe-Austerman S., Lantz K.;
RT "Draft genome sequence of a Pasteurellaceae bacterium isolated from a pygmy
RT hippo (Hexaprotodon liberiensis).";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC HypE, it catalyzes the synthesis of the CN ligands of the active site
CC iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC using carbamoylphosphate as a substrate and transferring the
CC carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC {ECO:0000256|PIRNR:PIRNR006256}.
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 ECO:0000256|PIRNR:PIRNR006256};
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, ECO:0000256|PIRNR:PIRNR006256}.
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:OOH88809.1}.
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DR EMBL; MQVI01000028; OOH88809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3TQT9; -.
DR STRING; 1924934.BMT54_08280; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000188845; 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 Reference proteome {ECO:0000313|Proteomes:UP000188845};
KW Transferase {ECO:0000313|EMBL:OOH88809.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 202..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 761 AA; 84906 MW; 16056A3660C50DDF CRC64;
MKFIELRIKG KVQGVGFRPF VWLLAKELQL KGDVNNDGQG VLIRFQAPTE AQLTRFIQDL
TEKLPPLAKI TDIQQQEKQI ETLPYFEDFT IRESENNAMD TQIVPDAATC PTCIAELFDP
NNRRFHYPFT NCTHCGPRFT IIRAIPYDRP NTSMADFPFC PECETEYKDP ADRRFHAQPN
ACPSCGPHIW LQNKTNQLAT HEDALQQTVE LLIQGKIVAI KGLGGFHLAC DATNSDAVNL
LRQRKNRPNK PLAVMVPTLN FLTDLVPEEQ QLLTSSAAPI VLLKKHKAPR LCEQIALNLA
EVGIMLPSNP LQHLLLNQAN RPLVMTSANP SGEPPVLDNR DAIEKLGSLA DFYLCHNRDI
LQRADDSLVR FAFDGLETLR RARGYVPDET ELNITAQRHI LALGSDLKNT FCLQKGNKAV
VSQHIGDTSN LKVQKQLNDN LQLFQQIYQF QPNALAVDAH SGYFSSQIGK QLASEQQLPI
YEVLHHHAHI SAVLAEHHCN DKVIGIALDG IGMGENEQLW GGECLLVDKH HCQHLGGLPP
VALAGGDLAA KQPWRNWLAH IQQFLPNWQE IANSTLQPFN WQILARAIEA KINSPVISST
GRLFDAVAYA LGIAPNQLSW EGEAACHLET LASQSQWVHK SIVQIKSTLN IAMPIGDNNQ
LDLATFWRTW LNLDCSVEDK AFAFHFALAT GFADMARENA QKYGCQTIVL SGGVMHNQLL
RQLLKENLSD FNVLSGQQYP MNDGGLSLGQ SWIVGHLIES N
//
