ID A0A0W0TSB2_9GAMM Unreviewed; 742 AA.
AC A0A0W0TSB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:KTC98487.1};
GN ORFNames=E4T54_10370 {ECO:0000313|EMBL:QBS13108.1}, Lgee_1564
GN {ECO:0000313|EMBL:KTC98487.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC98487.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTC98487.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC98487.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBS13108.1, ECO:0000313|Proteomes:UP000294523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1308 {ECO:0000313|EMBL:QBS13108.1,
RC ECO:0000313|Proteomes:UP000294523};
RA Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA Charpentier X.;
RT "Diverse conjugative elements silence natural transformation in Legionella
RT species.";
RL Submitted (MAR-2019) 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}.
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DR EMBL; LNYC01000063; KTC98487.1; -; Genomic_DNA.
DR EMBL; CP038271; QBS13108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0TSB2; -.
DR STRING; 45065.Lgee_1564; -.
DR KEGG; lgt:E4T54_10370; -.
DR PATRIC; fig|45065.4.peg.1697; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR Proteomes; UP000294523; 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:UP000054785};
KW Transferase {ECO:0000313|EMBL:QBS13108.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 5..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 187..375
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 742 AA; 81239 MW; 7E019293C3427CDB CRC64;
MSMQRLKIGI RGRVQGVGFR PHVFMLAKTL NLTGFVRNCG EGVILEIQGK NAHAFLDALP
GNLPPLARID ACDITESACI ADEACFTILE SLQEHANTII APDTAPCDAC LQELFNPQSR
YFQYPFLNCT HCGPRLTITE GLPYDRARTA MHCFPLCGAC LAEYHDPENR RYHAQPIACE
ACGPALERDI ETIASALKKG KIVALKGPGG YQLLCDARNT SALSTLRARK QREQKPFAVM
VQNVEVAACF TEVDATAKEL LESRARPIVL LKKRLPERLS DAIAPNLSHL GIMLPATPLH
HLLFKVMNIS HAALVVTSAN ISGNPLIIDD EIAKTALSAI ADIIISHNRD ILTRVDDSVV
TIINNAPVFI RRARGFVPER IELPMRIPST LALGGHLKNT FCITRDDEAF VSQHIGSLTN
RETIAFLHES IDYWRRFLNA DIERVACDWH PDFYTSRLAE SFNLPVTPVQ HHHAHLASVA
AEHGLKEPAL GLALDGYGYG FEGDAWGGEL FILEETRFER IGHFEPLPLP GGERAAREPW
RMGAAVLHQL DMNARIATKF AHMPQAALLA GHLKQATKIP NTSSCGRLFD AASALTGVCL
MSQYEGQAAM QLESLVAMPI VHPNGWRITN NRFSMLAVFK ELLSLCPVEG ASLFHGTLIA
GLSEWLLTNA HKYRLSTILL SGGCFLNKVL TEGLYSRLTQ SGLQVYLPER LPPNDGGLSL
GQAFIAGAGD VSGHAGSNHK NS
//
