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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 sulfurtransferase (EC 2.8.1.11) (Sulfurtransferase uba4) (Sulfur carrier protein MOCS2A sulfurtransferase); Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase)]

 A0A063C4A1_9HYPO        Unreviewed;       478 AA.
A0A063C4A1;
03-SEP-2014, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 1.
22-NOV-2017, entry version 29.
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=Adenylyltransferase uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03049};
Name=uba4 {ECO:0000256|HAMAP-Rule:MF_03049};
Synonyms=cnxF {ECO:0000256|HAMAP-Rule:MF_03049};
ORFNames=UV8b_2753 {ECO:0000313|EMBL:KDB16297.1};
Ustilaginoidea virens.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales;
Hypocreales incertae sedis; Ustilaginoidea.
NCBI_TaxID=1159556 {ECO:0000313|EMBL:KDB16297.1, ECO:0000313|Proteomes:UP000027002};
[1] {ECO:0000313|EMBL:KDB16297.1, ECO:0000313|Proteomes:UP000027002}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UV-8b {ECO:0000313|EMBL:KDB16297.1,
ECO:0000313|Proteomes:UP000027002};
Zhang Y., Zhang K., Fang A., Han Y., Yang J., Xue M., Bao J., Hu D.,
Zhou B., Sun X., Li S., Wen M., Yao N., Ma L.-J., Liu Y., Zhang M.,
Huang F., Luo C., Zhou L., Li J., Chen Z., Miao J., Wang S., Lai J.,
Xu J., Hsiang T., Peng Y.-L., Sun W.;
"Specific adaptation of Ustilaginoidea virens in occupying host
florets revealed by comparative and functional genomics.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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|HAMAP-Rule:MF_03049,
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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KDB16297.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; JHTR01000011; KDB16297.1; -; Genomic_DNA.
EnsemblFungi; KDB16297; KDB16297; UV8b_2753.
UniPathway; UPA00344; -.
UniPathway; UPA00988; -.
Proteomes; UP000027002; 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:UP000027002};
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:UP000027002};
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 373 476 Rhodanese. {ECO:0000259|PROSITE:PS50206}.
NP_BIND 124 128 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
NP_BIND 185 186 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
COILED 5 39 {ECO:0000256|SAM:Coils}.
ACT_SITE 245 245 Glycyl thioester intermediate; for
adenylyltransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
ACT_SITE 431 431 Cysteine persulfide intermediate; for
sulfurtransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 228 228 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 231 231 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 323 323 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 326 326 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 96 96 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 117 117 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 141 141 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
SEQUENCE 478 AA; 52810 MW; F2908133F3DC67B1 CRC64;
MDDNIDRLRE EIAQREAELA GLKSRLAAAE QSRQQQQQQQ QQHHHHHHRQ HVEPWKWPLE
ALEYQRYGRQ MIVPKFGLEA QLRLKKARVL LVGAGGLGCP AAAYLAGSGV GALGLVDGDT
VELSNLHRQV AHSTSRVGMS KTESAIAFLR DLNAGVTYEG HGVHLTADNA EDIVSRYDLV
LDCTDRPASR YLISDICVLL GKPLISASAF QTSGQLIVLN SPPGRGPCYR CVFPKPPPPE
TVVGCGEGGI IGPVVGVMGV LQALEAVKLI CRGGPEAGLE ASPDEERHHH QQQQQQHTML
LFSGMADHCP FRSVRMRGKR QGCFSCSENP QLTADYLKTA MDYVQFCGST RPVQLLPRQE
RISAQEYRLL SERGTKHVLL DVREREHFHL AHIPGSINVP MSRFTSLGSR DALPEEFPRD
LPAHVPVYVV CRVGNDSQVA ARRLKELGLS RNGERFVGDI VGGLRSWKDT VDGSLPFL


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