HYPF2_CUPNH
ID HYPF2_CUPNH Reviewed; 807 AA.
AC O07451; Q7WXM7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Carbamoyltransferase HypF2 {ECO:0000250|UniProtKB:P30131};
DE EC=6.2.-.- {ECO:0000250|UniProtKB:P30131};
DE AltName: Full=Carbamoyl phosphate-converting enzyme hypF2;
DE AltName: Full=[NiFe]-hydrogenase maturation factor hypF2;
DE Short=Hydrogenase maturation protein hypF2;
GN Name=hypF2; OrderedLocusNames=PHG096;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9799289; DOI=10.1007/s002030050666;
RA Wolf I., Buhrke T., Dernedde J., Pohlmann A., Friedrich B.;
RT "Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in
RT Alcaligenes eutrophus H16.";
RL Arch. Microbiol. 170:451-459(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
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:0000250|UniProtKB:P30131}.
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:0000250|UniProtKB:P30131};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000250|UniProtKB:P30131}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000305}.
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DR EMBL; AF002655; AAB60890.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85849.1; -; Genomic_DNA.
DR RefSeq; WP_011154018.1; NZ_CP039289.1.
DR AlphaFoldDB; O07451; -.
DR SMR; O07451; -.
DR STRING; 381666.PHG096; -.
DR EnsemblBacteria; AAP85849; AAP85849; PHG096.
DR GeneID; 39976777; -.
DR KEGG; reh:PHG096; -.
DR PATRIC; fig|381666.6.peg.73; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_4; -.
DR OMA; VQHHYAH; -.
DR OrthoDB; 48295at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro.
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; YrdC-like_dom.
DR InterPro; IPR011125; Znf_HypF.
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; SSF54975; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00143; hypF; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Ligase; Metal-binding; Plasmid; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..807
FT /note="Carbamoyltransferase HypF2"
FT /id="PRO_0000071615"
FT DOMAIN 14..101
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT DOMAIN 212..415
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT ZN_FING 120..145
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT ZN_FING 170..195
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 65..68
FT /note="ELRE -> DSRLR (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> D (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..300
FT /note="RS -> H (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> T (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 554..570
FT /note="LLLVDGGACKRLGHLRE -> TAAGGRRRLLAPRSLAR (in Ref. 1;
FT AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="S -> R (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="Missing (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 720..727
FT /note="TNAARGAA -> NECRARRS (in Ref. 1; AAB60890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 86438 MW; 5087D2C08F783DE7 CRC64;
MLMPRRPRNP RTVRIRIRVR GVVQGVGFRP FVYRLARELG LAGWVRNDGA GVDIEAQGSA
AALVELRERL RRDAPPLARV DEIGEERCAA QVDADGFAIL ESSRSDAAVH TAIGHDTAVC
PDCLAELFDP ANRRYRYAFI NCTQCGPRYT LTWALPYDRA TTSMAPFPQC RPCLDEYNAP
EHRRFHAEPN ACPDCGPSLA LLNAQGMPVE DVDPIAETVA RLQRGEIVAI KGLGGFHLAC
DAHNADAVAR LRSRKQREEK PFAVMVANLA TAAQWGDIGS GEAALLTASE RPIVLLRKRS
GVDGRFAGVA PGLVWLGVML PYTPLQYLLF HEAAGRPEGL GWLAQPQSLV LVMTSANPGG
EPLVTGNDEA AQRLTGIADA FLLHDREILV RCDDSVVRGD GEPAPHVQFI RRARGYTPRA
IKLARSGPSV LALGGSFKNT VCLTRGDEAF VSQHVGDLGN AATCEALIEA VAHLQRVLEI
RPQLVAHDLH PDFFSTRHAA ELAAQWGVPA VAVQHHHAHI AAVLAEHGSD EPAIGLALDG
VGLGDDGQAW GGELLLVDGG ACKRLGHLRE LPLPGGDRAA REPWRMAAAA LHAMGRGEEI
EGRFPRQPGA PMVNRMLAQR LNAPLSSSMG RWFDAAAGLL GTRETMAYEG QAAMLLEGLA
ESWGEQPSPG RPKTVAHSLG GVPRSGGGTY KALALPDAWR IDAGNTLDLL PLLEALSAET
NAARGAAQFH ATLVAALEAW TVATVQVTGV RTVVFGGGCF LNHILARNLC RRLAARGLTV
LTARQLPPND GGIALGQVWV ALQRAPN
