ID N4TVJ4_FUSC1 Unreviewed; 448 AA.
AC N4TVJ4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Adenylyltransferase and sulfurtransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein F {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000256|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049};
DE EC=2.7.7.80 {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Adenylyltransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049};
DE EC=2.8.1.11 {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfurtransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049};
GN Name=uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
GN Synonyms=cnxF {ECO:0000256|HAMAP-Rule:MF_03049};
GN ORFNames=FOC1_g10009182 {ECO:0000313|EMBL:ENH63287.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH63287.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC essential during biosynthesis of the molybdenum cofactor. Acts by
CC mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and
CC MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-
CC adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-
CC COSH) of their C-terminus. The reaction probably involves hydrogen
CC sulfide that is generated from the persulfide intermediate and that
CC acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient
CC disulfide bond is formed. Does not use thiosulfate as sulfur donor;
CC nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
CC {ECO:0000256|HAMAP-Rule:MF_03049}.
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC essential during biosynthesis of the molybdenum cofactor. Acts by
CC mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and
CC mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-
CC adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-
CC COSH) of their C-terminus. The reaction probably involves hydrogen
CC sulfide that is generated from the persulfide intermediate and that
CC acts as a nucleophile towards urm1 and mocs2a. Subsequently, a
CC transient disulfide bond is formed. Does not use thiosulfate as sulfur
CC donor; nfs1 probably acting as a sulfur donor for thiocarboxylation
CC reactions. {ECO:0000256|ARBA:ARBA00043893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] =
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-
CC CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase];
CC Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03049};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03049};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03049};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03049}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03049}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC family. UBA4 subfamily. {ECO:0000256|HAMAP-Rule:MF_03049}.
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DR EMBL; KB731255; ENH63287.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TVJ4; -.
DR STRING; 1229664.N4TVJ4; -.
DR VEuPathDB; FungiDB:FOC1_g10009182; -.
DR HOGENOM; CLU_013325_1_2_1; -.
DR OMA; IPDVGMD; -.
DR UniPathway; UPA00344; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061604; F:molybdopterin-synthase sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
DR CDD; cd01526; RHOD_ThiF; 1.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR HAMAP; MF_03049; MOCS3_Uba4; 1.
DR InterPro; IPR028885; MOCS3/Uba4.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03049}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03049};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03049};
KW Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_03049};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_03049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03049}; Nucleotidyltransferase {ECO:0000313|EMBL:ENH63287.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03049};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03049};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03049}.
FT DOMAIN 344..446
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT COILED 4..38
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 229
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT ACT_SITE 401
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 108..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 169..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
SQ SEQUENCE 448 AA; 48997 MW; 1D86CDA9823AB0BB CRC64;
MEEIDNLRRE IAKREVELAD LRSQLAAAES QARESKEAWK WPLDNHEYER YSRQMIVPNF
GLQGQLRLRN AKVLLVGAGG LGCPAAAYLA GSGIGTIGLV DGDEVEVSNL HRQVAHSTGR
VGMSKVQSAI TYLKDLNPTI TYNAHNTHLT PQNSEDIVSG YDLVLDCTDH PTSRYLISDI
CVLLSKPLVS ASAFQTSGQL IVLNNPPGKG PCYRCVFPTP PPPDSVVGCG EGGIIGPIVG
TMGILQALEA IKLISRGDLE THGEAKTPML LLFSGMADTP FRSVRMRGRR KTCLACGDEN
RLTLDELKNS MDYVQFCGVK QPVQLLKPDE RVTAKEYDEL SKLENKDMLL VDVREKEHFD
LCNISGSVNI PISRFMSARG EATPEGWPSD LPHSTPIYVV CRVGNDSQIA AQKLKDLGLG
NNGERFIGDI LGGIKSWKDT VDPSVPFI
//
