ID A0A1J9Q3S0_9EURO Unreviewed; 558 AA. AC A0A1J9Q3S0; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 05-DEC-2018, entry version 18. 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=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049}; DE AltName: Full=Adenylyltransferase uba4 {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=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049}; DE AltName: Full=Sulfurtransferase uba4 {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 CC tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and CC tRNA(Gln). Also essential during biosynthesis of the molybdenum CC cofactor. Acts by mediating the C-terminal thiocarboxylation of CC sulfur carriers urm1 and MOCS2A. Its N-terminus first activates CC urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide CC sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A CC to form thiocarboxylation (-COSH) of their C-terminus. The CC reaction probably involves hydrogen sulfide that is generated from CC the persulfide intermediate and that acts as nucleophile towards CC urm1 and MOCS2A. Subsequently, a transient disulfide bond is CC formed. Does not use thiosulfate as sulfur donor; nfs1 probably CC 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- CC terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur- CC carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; CC Xref=Rhea:RHEA:43616, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778, CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202; EC=2.7.7.80; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03049}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C- CC terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine CC desulfurase] = [molybdopterin-synthase sulfur-carrier protein]- CC C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl- CC [cysteine desulfurase]; Xref=Rhea:RHEA:48612, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, CC ChEBI:CHEBI:90619, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160; EC=2.8.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03049}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03049}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03049}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03049}. CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine- CC tRNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03049, CC ECO:0000256|SAAS:SAAS00337567}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049, CC ECO:0000256|SAAS:SAAS00135658}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC HesA/MoeB/ThiF family. UBA4 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_03049, ECO:0000256|SAAS:SAAS00535337}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0018192; P:enzyme active site formation via cysteine modification to L-cysteine persulfide; IEA:UniProtKB-UniRule. 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 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; IPR000594; ThiF_NAD_FAD-bd. DR InterPro; IPR035985; Ubiquitin-activating_enz. DR Pfam; PF00899; ThiF; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR SUPFAM; SSF69572; SSF69572; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885939}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000182235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00416191}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00001785}; KW Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_03049}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00416195}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885830}; KW Reference proteome {ECO:0000313|Proteomes:UP000182235}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00885834}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049, KW ECO:0000256|SAAS:SAAS00416193}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03049, ECO:0000256|SAAS:SAAS00001782}. FT DOMAIN 412 556 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT NP_BIND 130 134 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT NP_BIND 191 192 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT COILED 1 42 {ECO:0000256|SAM:Coils}. FT ACT_SITE 269 269 Glycyl thioester intermediate; for FT adenylyltransferase activity. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT ACT_SITE 511 511 Cysteine persulfide intermediate; for FT sulfurtransferase activity. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 252 252 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 255 255 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 341 341 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT METAL 344 344 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 102 102 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 123 123 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}. FT BINDING 147 147 ATP. {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 //