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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) (Sulfur carrier protein MOCS2A adenylyltransferase) (Adenylyltransferase uba4); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfurtransferase uba4) (Sulfur carrier protein MOCS2A sulfurtransferase)]

 M2QXC4_COCSN            Unreviewed;       526 AA.
M2QXC4;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
01-MAY-2013, sequence version 1.
25-APR-2018, entry version 43.
RecName: Full=Adenylyltransferase and sulfurtransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein F {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000256|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049};
EC=2.8.1.11 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Sulfurtransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049};
EC=2.7.7.80 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Adenylyltransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
Name=uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
Synonyms=cnxF {ECO:0000256|HAMAP-Rule:MF_03049};
ORFNames=COCSADRAFT_100535 {ECO:0000313|EMBL:EMD59714.1};
Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot
and spot blotch fungus) (Bipolaris sorokiniana).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
Pleosporaceae; Bipolaris.
NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD59714.1, ECO:0000313|Proteomes:UP000016934};
[1] {ECO:0000313|EMBL:EMD59714.1, ECO:0000313|Proteomes:UP000016934}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
"Diverse lifestyles and strategies of plant pathogenesis encoded in
the genomes of eighteen Dothideomycetes fungi.";
PLoS Pathog. 8:E1003037-E1003037(2012).
[2] {ECO:0000313|Proteomes:UP000016934}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
Grigoriev I.V., Zhong S., Turgeon B.G.;
"Comparative genome structure, secondary metabolite, and effector
coding capacity across Cochliobolus pathogens.";
PLoS Genet. 9:E1003233-E1003233(2013).
-!- 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.
{ECO:0000256|HAMAP-Rule:MF_03049}.
-!- CATALYTIC ACTIVITY: ATP + [molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-
carrier protein]-Gly-Gly-AMP. {ECO:0000256|HAMAP-Rule:MF_03049}.
-!- CATALYTIC ACTIVITY: [Molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-
cysteine = AMP + [molybdopterin-synthase sulfur-carrier protein]-
Gly-NH-CH(2)-C(O)SH + cysteine desulfurase. {ECO:0000256|HAMAP-
Rule:MF_03049}.
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03049}.
-!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
tRNA biosynthesis. {ECO:0000256|SAAS:SAAS00337567}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00135658}.
-!- SIMILARITY: In the N-terminal section; belongs to the
HesA/MoeB/ThiF family. UBA4 subfamily.
{ECO:0000256|SAAS:SAAS00535337}.
-----------------------------------------------------------------------
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EMBL; KB445652; EMD59714.1; -; Genomic_DNA.
RefSeq; XP_007704708.1; XM_007706518.1.
EnsemblFungi; EMD59714; EMD59714; COCSADRAFT_100535.
GeneID; 19129704; -.
KEGG; bsc:COCSADRAFT_100535; -.
KO; K11996; -.
OrthoDB; EOG092C3K3Z; -.
UniPathway; UPA00344; -.
UniPathway; UPA00988; -.
Proteomes; UP000016934; Unassembled WGS sequence.
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:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
GO; GO:0018192; P:enzyme active site formation via cysteine modification to L-cysteine persulfide; IEA:UniProtKB-UniRule.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
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; 1.
PROSITE; PS50206; RHODANESE_3; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885939}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000016934};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416191};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00001785};
Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_03049};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416195};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885939};
Reference proteome {ECO:0000313|Proteomes:UP000016934};
Transferase {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885834};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416193};
Zinc {ECO:0000256|HAMAP-Rule:MF_03049, ECO:0000256|SAAS:SAAS00001782}.
DOMAIN 411 524 Rhodanese. {ECO:0000259|PROSITE:PS50206}.
NP_BIND 159 163 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
NP_BIND 220 221 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
COILED 5 35 {ECO:0000256|SAM:Coils}.
ACT_SITE 286 286 Glycyl thioester intermediate; for
adenylyltransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
ACT_SITE 479 479 Cysteine persulfide intermediate; for
sulfurtransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 269 269 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 272 272 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 349 349 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 352 352 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 131 131 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 152 152 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 176 176 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
SEQUENCE 526 AA; 56980 MW; E6761D19D8B2B856 CRC64;
MTAVVSSLRK QIAACEATLQ ELRQQLAEAE QNQNQPSKVV PQKRPLATDP TNPLDHDMNF
GVPDDFRSEV FAILDQGEKK VKHAESEETQ KWELEKDEYK RYGRQLIMPE IGLQGQLRLK
SARVLIVGVG GLGCPAAAYL VGAGVGTVGL VDGDVVEESN LHRQILHSTA RVGMTKVESA
MVGLKSLNPN VNLVPHISRL SPETAISTFS GYDLVLDCTD TPASRYLISD ACVLLGKPLV
SASALRIDGQ LMVLNNPPLP PGDLNGGPCY RCVFPKPPPP ESVVSCGDGG ILGPVVGVMG
VLQALEAIKV LTQKTPAATP ADPPSLLIFS AYSNPMFRSI RLRSRKAKCA SCSANATVTK
QALEYGNLDY VQFCGSVLAP DNLLSPEERI SAQNYARLRS GVNPHTGTVS NRNSHILVDV
REKVQFELCH IDGSMNVPFS TVSSTPGPSA NKGHNGGDFE ENDWVTQLKQ SERPIFVICR
LGNDSQVTVK KMKELGLDLG GKRYIGDIKG GLQSWRKDIE TDFPDY


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