ID A0A0P0UQ11_9GAMM Unreviewed; 788 AA.
AC A0A0P0UQ11;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:BAS67260.1};
GN ORFNames=BSEPE_0244 {ECO:0000313|EMBL:BAS67260.1};
OS endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS67260.1, ECO:0000313|Proteomes:UP000067399};
RN [1] {ECO:0000313|EMBL:BAS67260.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67260.1,
RC ECO:0000313|Proteomes:UP000067399};
RA Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT mussels: influence on host distributions.";
RL Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN [2] {ECO:0000313|EMBL:BAS67260.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67260.1,
RC ECO:0000313|Proteomes:UP000067399};
RX PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA Hirano T., Maruyama T., Yoshida T.;
RT "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT symbiont population.";
RL ISME J. 10:990-1001(2016).
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; AP013042; BAS67260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0UQ11; -.
DR STRING; 1303921.BSEPE_0244; -.
DR KEGG; ebh:BSEPE_0244; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000067399; Chromosome.
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:UP000067399};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 23..111
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 220..404
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 788 AA; 87952 MW; 60D5E748E686F093 CRC64;
MNPRLIKSQQ TKKNKPNIKT LISKKITITG AVQGVGFRPF VYKIARQFNL VGEVYNDSAG
VVVIVQCTQI QLDQFLSLLK SDVPMLAKIA NINIENDYQS NQFYDDFSIG QSSKGEISAI
VLPDASICKD CIADITDKNN RRYGYAFTNC TNCGPRFSII KEIPYDRNST SMSVFSMCEQ
CKKEYQNPVN RRFHAQPNAC ADCGPQLQLT DMHGNDIVVD NIIKETVSLL KQGKIVAIKG
IGGFHLACLA SIEFAVVALR ERKHRKHKPF ALMAKNLSMV KQYCFVSDQE ECLLTDKASP
IVLLNKANDR LPDQIAPKQK NLGFMLPYSP LHYLLLQELG EPLVLTSGNQ SHNPQIIDNQ
HALNELESIA DYFLMHNRDI VNRVDDSVVQ YVAGDLRVIR RARGYGPTSL SLPKGFSSHS
GLLAVGAELK NTFCLLTESQ AIVSQHIGDL KTLESYQDFQ NNIDLYQQLY SAKIKQLACD
LHPEYLSSKY ADNYAQTNNI KLEAIQHHHA HIAACLFEHG GAIDSDKVLG VVWDGIGLGG
DNSLWGGEFL LADYVGFKRL AQFEYVPLLG GDKAATQPWR MAYAYFKHYN LELGDFFTNK
PTQDLEALLG SNIPLNLTSS VGRLFDAVAY VLGICPKHIS YEAQAAIELE SLAKSCCYDN
NAKLEGYEFE LKTTSSHCQI DIKQIWLGIL LDLKNQVECS IIAYKFHLCL ARLLFEITQQ
LKQDYLFETV VLSGGVFNNK LLLALTCELF NKIDGITLLT PSQLPFGDGG ISLGQAAICR
AREKKYGE
//
