ID L0DVS4_THIND Unreviewed; 821 AA.
AC L0DVS4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF2 [H] {ECO:0000313|EMBL:AGA33704.1};
GN OrderedLocusNames=TVNIR_2043 {ECO:0000313|EMBL:AGA33704.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA33704.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) 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; CP003989; AGA33704.1; -; Genomic_DNA.
DR RefSeq; WP_015258829.1; NC_019902.2.
DR AlphaFoldDB; L0DVS4; -.
DR STRING; 1255043.TVNIR_2043; -.
DR KEGG; tni:TVNIR_2043; -.
DR PATRIC; fig|1255043.3.peg.2065; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_6; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000010809; 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; 1.10.357.160; -; 1.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 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; 2.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..98
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 207..409
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 24
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 821 AA; 87963 MW; 6489C701F1D927F8 CRC64;
MIIRTDPIRR HVRVRGQVQG VGFRPYVYGL AVELGLTGWV LNDAAGVDLE IQGDPQAVAD
FLRRIAAEAP PLARVDAVET TERAPEPPDG EPAFRIAPSR AGAVRTGITP DAAVCAACLE
ELFDPNDRRY RYPFINCTHC GPRYTLTRAL PYDRPNTSMA AFSQCPPCQH EYDDPAHRRF
HAQPNACPDC GPRLTLLKPD GAPIAAADPL AETVRRLKAG EILAVKGLGG FHLLCDARNA
DSVARLRARK HREEKPLAVM AADLRALDGL VEIGDAEEQL LRSRDRPIVL LRKARECDET
LPGVAPGLAW LGAMLAYTPL HYLLFHEAAG RPVGTAWLEA EDVDPWLLVC TSANPGGEPL
VTDNAEAVQR LAGIADALLV HDRDILVRCD DSVIRVGAGG AAFLRRARGY TPNAIRLPHS
GPSVLALGAW LKNTLCVTRD DQAFLSPHIG DLDNAATCRS LDDSARHLLG ILEIRPERIA
CDQHPDFYSS QLAAAMAAEL DVPLIRVQHH HAHLAAVQAE HGLEGPVLGI AMDGVGLGSD
GTPWGGELLR LDGADFERLG HLAPLALPGG DRAAREPWRM AAAALHALGR GGEVAARFPE
QPLAVQLAEV LERGIHSPLS TSLGRHFDAA AGLLGLKPVQ RFEGQAAMLL EGLAEWYGHA
EPVADGWHIE ADHSLNLLPL LAWLADVGQP GGAPLRPTGV QVPTSGNTGT SFRTSNDAAT
EHGCSPPLSF TRDRCARQAY AAAVFHATLA AALAGWIGPV AEATGIRHLV FSGGCVLNQV
LMTELERRLT AVDVHVHLPR LAPANDGGLS LGQAWIAMNA R
//
