ID Q7WXP6_CUPNH Unreviewed; 796 AA.
AC Q7WXP6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF3 {ECO:0000313|EMBL:AAP85825.1};
GN OrderedLocusNames=PHG072 {ECO:0000313|EMBL:AAP85825.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1 {ECO:0000313|EMBL:AAP85825.1,
OG ECO:0000313|Proteomes:UP000008210}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:AAP85825.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:AAP85825.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RC PLASMID=megaplasmid pHG1 {ECO:0000313|EMBL:AAP85825.1,
RC ECO:0000313|Proteomes:UP000008210};
RX PubMed=12948488; DOI=10.1016/S0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
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}.
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DR EMBL; AY305378; AAP85825.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WXP6; -.
DR KEGG; reh:PHG072; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_4; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; 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; 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 Plasmid {ECO:0000313|EMBL:AAP85825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008210};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..86
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 196..384
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 11
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 796 AA; 84618 MW; 7A3D82CEB4B25D10 CRC64;
MRGMVQGVGF RPTVWRLAHD CGLSGSVRND SDGVQIRAWG DAVALDRFIA RLRDECPPLA
RIDAIERRVL AQDAEGADLG GFRIVASVGG PVRTGVVPDA VVCSACIADI GDPLNRRYRY
PFANCTHCGP RLSIVRAIPY DRANTAMAAF PMCPACLAEY EDPADRRFHA QPLACAACGP
HVWLEHTGGP LAAGPDDAIR AAWALLRDGG IVAIKGIGGF QLACDACNPV AVARLRQRKR
RERKPFALMA RDLAVIRQYS EPTAAECGLL QSPAAPIVIV QTRSDRQGAP LAPDVAPGIA
ALGFMLPGTP LHWLLMAMAD RPIVLTSGNA SDEPQCTENA DARMRLGAIA DAFLMHDRDV
VRRVDDSVAR VVLDVPRVMR RSRGYAPAPL PLPPGFAAAA PVLAMGGELK NTFCLMRAGE
AILSHHMGDL EDALTHADYR RALTQYMALF EHGPHLVAVD MHPEYLSGKI GRDLARQGQL
PVAQVQHHHA HIAACMAENR VALAAGPVLG VALDGIGYGV DGSLWGGEFL LADYRDFTRL
ACFKPVGMPG GERAIHQPWR NTYAHLAAAV GWDTLIARHA SLALVRFLAT RPREVLDAML
TRSINSPLAS SAGRLFDAVA AAAGVCPERA CYEGQAAMEF EALADRRTLS EEDDGRAYPF
AIVPGTPACL EPGPMWVALL ADLARATPAP LISARFHKGL AIAIASMVAY LADCPGAGCR
AVPVALSGGV FQNRILLEQV ATRLSAQGRR VLTHSQVPAN DGGLSFGQAA IAAARSLGGA
DVAGQANAGY RSTTCA
//
