ID A0A1J9Q3S0_9EURO Unreviewed; 558 AA. AC A0A1J9Q3S0; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 08-NOV-2023, entry version 35. 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=AJ78_08917 {ECO:0000313|EMBL:OJD09805.1}; OS Emergomyces pasteurianus Ep9510. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces. OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD09805.1, ECO:0000313|Proteomes:UP000182235}; RN [1] {ECO:0000313|EMBL:OJD09805.1, ECO:0000313|Proteomes:UP000182235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD09805.1, RC ECO:0000313|Proteomes:UP000182235}; RG The Broad Institute Genomics Platform; RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K., RA McEwen J.G.; RT "Emmonsia species relationships and genome sequence."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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 -!- 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}. 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:OJD09805.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LGRN01001122; OJD09805.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1J9Q3S0; -. DR STRING; 1447872.A0A1J9Q3S0; -. DR OrthoDB; 53913at2759; -. DR UniPathway; UPA00344; -. DR UniPathway; UPA00988; -. DR Proteomes; UP000182235; 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:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro. 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; 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; PF00899; ThiF; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1. DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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}; Reference proteome {ECO:0000313|Proteomes:UP000182235}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03049}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03049}. FT DOMAIN 412..556 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT REGION 446..478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1..42 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 269 FT /note="Glycyl thioester intermediate; for FT adenylyltransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT ACT_SITE 511 FT /note="Cysteine persulfide intermediate; for FT sulfurtransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 130..134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 147 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 191..192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 341 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" FT BINDING 344 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049" SQ SEQUENCE 558 AA; 60304 MW; B71A0609F5642162 CRC64; MKNLLKSREL LQQQIATAET QLSLLKAELE RMERQIAAEA ITTSGRPDQV NEGKTVPVPK RRYPLEQDEY RRYGRQMIVE QIGLEGQLKL RASSVLIVGA GGLGCPAAMY LAGAGIGTIG IVDGDTVEAS NLHRQVLHRT RNVGRFKVDS AIEYLKELNP HPKYIPYHTH LTPADAPSIF TPYDIILDCT DNPATRYLIS DTAVLLGKPL VSASALRTEG QLMVLNYPPQ NPSGTLSNST NDTNDTSNGG PCYRCVFPKP PPAASVTSCA DGGILGPVVG VMGVLQALET IRVLTHTTQR ADKTTSTATA TTTIAPTLHL FSAFSSPPFR SIRLRPRRRD CAACSLAART ITLDSLRSGS MDYVQFCGGV VGPETLLGAE ERISASEYWR RYRELQQEPE REGNAEVEAE GEVDRPILID VREAVQYGLA ALEGSVNIPI SQILSSTSSS SSSSSSSSSS SSSSSSSSSS SSSPTSMARS TAESTVSSNF PSWYPSSLFD TCPTKPIHVV CRLGNDSQVA VRKLKELGVD RGGERWVGDI QGGLRAWRDE VEAEFPDY //