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Database: UniProt
Entry: I7ZUC9_ASPO3
LinkDB: I7ZUC9_ASPO3
Original site: I7ZUC9_ASPO3 
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
//
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