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Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]

 UBA4_EMENI              Reviewed;         482 AA.
O59954; C8VNC5; Q5BAV3;
14-APR-2009, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 2.
20-JUN-2018, entry version 120.
RecName: Full=Adenylyltransferase and sulfurtransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein F {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000255|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
EC=2.7.7.80 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Adenylyltransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
EC=2.8.1.11 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Sulfurtransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
Name=uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
Synonyms=cnxF {ECO:0000255|HAMAP-Rule:MF_03049}; ORFNames=AN2327;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE
MOLYBDENUM COFACTOR, AND MUTAGENESIS OF GLY-82; GLY-100; ARG-130;
CYS-185; GLU-215 AND GLY-264.
PubMed=9614089; DOI=10.1074/jbc.273.24.14869;
Appleyard M.V.C.L., Sloan J., Kana'n G.J.M., Heck I.S., Kinghorn J.R.,
Unkles S.E.;
"The Aspergillus nidulans cnxF gene and its involvement in
molybdopterin biosynthesis. Molecular characterization and analysis of
in vivo generated mutants.";
J. Biol. Chem. 273:14869-14876(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
-!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at
tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and
tRNA(Gln). Also essential during biosynthesis of the molybdenum
cofactor. Acts by mediating the C-terminal thiocarboxylation of
sulfur carriers urm1 and mocs2a. Its N-terminus first activates
urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide
sulfur on the catalytic cysteine is transferred to urm1 and mocs2a
to form thiocarboxylation (-COSH) of their C-terminus. The
reaction probably involves hydrogen sulfide that is generated from
the persulfide intermediate and that acts as nucleophile towards
urm1 and mocs2a. Subsequently, a transient disulfide bond is
formed. Does not use thiosulfate as sulfur donor; nfs1 probably
acting as a sulfur donor for thiocarboxylation reactions (By
similarity). {ECO:0000250, ECO:0000269|PubMed:9614089}.
-!- CATALYTIC ACTIVITY: ATP + [molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-
carrier protein]-Gly-Gly-AMP. {ECO:0000255|HAMAP-Rule:MF_03049}.
-!- CATALYTIC ACTIVITY: [Molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-
cysteine + reduced acceptor = AMP + [molybdopterin-synthase
sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + [cysteine
desulfurase] + oxidized acceptor. {ECO:0000255|HAMAP-
Rule:MF_03049}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03049};
-!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03049}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
-!- SIMILARITY: In the N-terminal section; belongs to the
HesA/MoeB/ThiF family. UBA4 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03049}.
-!- SEQUENCE CAUTION:
Sequence=AAC24520.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CBF86614.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAA64438.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF055287; AAC24520.1; ALT_INIT; Genomic_DNA.
EMBL; AACD01000038; EAA64438.1; ALT_INIT; Genomic_DNA.
EMBL; BN001307; CBF86614.1; ALT_INIT; Genomic_DNA.
RefSeq; XP_659931.1; XM_654839.1.
ProteinModelPortal; O59954; -.
SMR; O59954; -.
STRING; 162425.CADANIAP00009021; -.
EnsemblFungi; EAA64438; EAA64438; AN2327.2.
GeneID; 2875088; -.
KEGG; ani:AN2327.2; -.
HOGENOM; HOG000281219; -.
InParanoid; O59954; -.
KO; K11996; -.
OrthoDB; EOG092C3K3Z; -.
UniPathway; UPA00344; -.
UniPathway; UPA00988; -.
Proteomes; UP000000560; Chromosome VII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0061604; F:molybdopterin-synthase sulfurtransferase activity; IEA:UniProtKB-EC.
GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
GO; GO:0042292; F:URM1 activating enzyme activity; IBA:GO_Central.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
Gene3D; 3.40.250.10; -; 1.
HAMAP; MF_03049; MOCS3_Uba4; 1.
InterPro; IPR028885; MOCS3/Uba4.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
InterPro; IPR000594; ThiF_NAD_FAD-bd.
InterPro; IPR035985; Ubiquitin-activating_enz.
Pfam; PF00581; Rhodanese; 1.
Pfam; PF00899; ThiF; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF69572; SSF69572; 2.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Metal-binding;
Molybdenum cofactor biosynthesis; Multifunctional enzyme;
Nucleotide-binding; Reference proteome; Transferase; tRNA processing;
Zinc.
CHAIN 1 482 Adenylyltransferase and sulfurtransferase
uba4.
/FTId=PRO_0000369226.
DOMAIN 366 480 Rhodanese. {ECO:0000255|HAMAP-
Rule:MF_03049}.
NP_BIND 126 130 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
NP_BIND 187 188 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
ACT_SITE 253 253 Glycyl thioester intermediate; for
adenylyltransferase activity.
{ECO:0000255|HAMAP-Rule:MF_03049}.
ACT_SITE 435 435 Cysteine persulfide intermediate; for
sulfurtransferase activity.
{ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 236 236 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 239 239 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 315 315 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 318 318 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 98 98 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 119 119 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 143 143 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
MUTAGEN 82 82 G->D: In cnxF21ts and cnxF24ts;
temperature-sensitive mutant. Impairs
molybdopterin biosynthesis.
{ECO:0000269|PubMed:9614089}.
MUTAGEN 100 100 G->S: In cnxF1285; impairs molybdopterin
biosynthesis.
{ECO:0000269|PubMed:9614089}.
MUTAGEN 130 130 R->Q: In cnxF200; impairs molybdopterin
biosynthesis.
{ECO:0000269|PubMed:9614089}.
MUTAGEN 185 185 C->Y: In cnxF472; impairs molybdopterin
biosynthesis.
{ECO:0000269|PubMed:9614089}.
MUTAGEN 215 215 E->K: In cnxF119; impairs molybdopterin
biosynthesis.
{ECO:0000269|PubMed:9614089}.
MUTAGEN 264 264 G->S: In cnxF142ts; temperature-sensitive
mutant. Impairs molybdopterin
biosynthesis.
{ECO:0000269|PubMed:9614089}.
SEQUENCE 482 AA; 52246 MW; 3D6C0F797B242812 CRC64;
MEDLETRCAS LRTEIAAAEA QLTKLKRELH EAEGAALRAQ SQKTASANAT TGQRTKSKWP
LHGEEYRRYG RQMIVPQFGL QGQLKLRDAK VLIVGAGGLG CPAALYLAGA GVGTIGLVDG
DTVEASNLHR QVLHRSRNVG KLKVDSAIEY LRELNPHPTY IAHQAHLTPR EAPDIFKDYD
LILDCTDNPA TRYLISDTAV LLGKPLVSAS ALRTEGQLMV LNNPPQPPGD KTGGPCYRCV
FPKPPPANSV TSCADGGILG PVVGTMGVLQ ASEAIKVLTS AGESVEATPP SLLIFSAYSS
PQFRTIKLRS RRPNCAVCSA EATVTLESVR SGSMDYVFFC GTVDPADILS PEERISPSEY
GNVDSAGAQR HIIDVREKVQ FDICSLENSI NIPMSTILAS AYSAPTLDAD EPKRLPSWLP
PEVAHESNKP IYVVCRQGND SQTVVRKLKE LGLDHGGERP VVDIKGGFRS WREQVDPDWP
DY


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