ID I7ZUC9_ASPO3 Unreviewed; 495 AA.
AC I7ZUC9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
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=Ao3042_08354 {ECO:0000313|EMBL:EIT75582.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT75582.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT75582.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT75582.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) 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:EIT75582.1}.
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DR EMBL; AKHY01000175; EIT75582.1; -; Genomic_DNA.
DR AlphaFoldDB; I7ZUC9; -.
DR HOGENOM; CLU_013325_1_2_1; -.
DR UniPathway; UPA00344; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000002812; 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; 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|HAMAP-Rule:MF_03049};
KW Cytoplasm {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}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049};
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 376..493
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT ACT_SITE 448
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 189..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03049"
SQ SEQUENCE 495 AA; 53381 MW; 90A40E70F834883C CRC64;
MGDIEDTCAS LRAQIAATEA QLAGLKRELE SAEQAAIKVR AQDAPNSTAT TSTQGNEKRK
WPLLDEEYRR YGRQMIVPQV GLQGQLKLRS AKVLIVGAGG LGCPAAQYLA GAGVGTLGLV
DGDTVESSNL HRQVLHRSKN VGKLKVDSAI ESLRDLNPHP TYIAHRAHLA PQDAADIFKN
YDLILDCTDN PATRYLISDT AVLLGKPLVS ASALRTEGQL MVLNNPPRSV GDKTGGPCYR
CVFPRPPPAN SIMSCADGGI LGPVVGTMGV LQALEAIKVI TATDEEVKPP SLHIFSAYSS
PLFRTIKLRS RRPNCAVCSS EASVTLETVK SGSTDYVFFC GSVGPEKLLL PEERISPREY
RTKYPVTASS EAIGTATKEP TIIDVREKVQ FDICSLENSI NIPISSILSS ATKTAQNNEV
SNGSNPLPPW LPADIASSDS IDPIYVVCRL GNDSQIAVKR LKELGLDRGG ERVVADIRGG
LRAWREQVDP EWPEY
//