ID A0A1M3HER5_9PROT Unreviewed; 740 AA.
AC A0A1M3HER5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=BGO60_09000 {ECO:0000313|EMBL:OJW56996.1};
OS Thiobacillus sp. 65-1059.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1895860 {ECO:0000313|EMBL:OJW56996.1, ECO:0000313|Proteomes:UP000184230};
RN [1] {ECO:0000313|EMBL:OJW56996.1, ECO:0000313|Proteomes:UP000184230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65-1059 {ECO:0000313|EMBL:OJW56996.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJW56996.1}.
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DR EMBL; MKUE01000012; OJW56996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HER5; -.
DR STRING; 1895860.BGO60_09000; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000184230; Unassembled WGS sequence.
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 Transferase {ECO:0000313|EMBL:OJW56996.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 202..387
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 740 AA; 79717 MW; B265E26C1FDA3F4B CRC64;
MPERVAQFIT IGGRVQGVGF RPFVYRLAQQ HGITGWVRNV DGAVEIHAEG EPVQLQRFND
ALLSEAPPLS APGPLAVTTC APAHAKAFSI LDSQSISAAD IHLPADGFVC ADCRAELHDP
VDRRHRYPFI NCTQCGPRYT LITALPYDRP NTAMRDFALC PDCRREYENP LDRRFHAEPI
ACPVCGPHLQ FVSGDATHDG DATALATAVA ALRAGKIVAV KGVGGYHLLC DATNAAAVAT
LRARKPRPAK PLAVMLRDLA ALRAVAHTTP DLEDFLASPE RPIVLLQKRV DSGLSEHIAP
GLAEIGCLLP YSPLHDLLLT DFDGPLVATS GNLSGEPVLT ENHEAQTRLA HLADAFLHHD
RPIVRPADDP VYRVIAGIPR PLRLGRGAAP LELELPAPLA EPVLALGSHM KNTLCLAWGR
RAVVSPHIGE LDTLRSLDTL AQVAADLQRL YQVQATKLLI DRHPGYGYRR YARDSGLPLT
EIWHHHAHAS ALAWEFPDVK EWIVFAWDGV GLGEDRTLWG GEAFTGSPGR WQRAASFRPF
RLPGGDKAGR EPWRAAAALL WESGRAAPFA PEPLQRAWSQ GINSPASSSL GRLFDAAAAL
IGVCAHASFE GEGPMRLEAV AAADGEPVAL PLARDATGIW RSDWAPLLPM LADIARPQAT
RAASFHLSLT QALLEQAQQL RAQTGITSVG LAGGVFQNRL LAEAAIGRLQ AAGFAAHLPQ
RVPVNDAGLS FGQVIEFLHP
//
