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MOCS3_DANRE
ID   MOCS3_DANRE             Reviewed;         459 AA.
AC   Q8AWD2; Q6IQE7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE   AltName: Full=Molybdenum cofactor synthesis protein 3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE              EC=2.7.7.80 {ECO:0000255|HAMAP-Rule:MF_03049};
DE     AltName: Full=Adenylyltransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE     AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE              EC=2.8.1.11 {ECO:0000255|HAMAP-Rule:MF_03049};
DE     AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE     AltName: Full=Sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
GN   Name=mocs3; Synonyms=uba4; ORFNames=zgc:55696;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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       (By similarity). {ECO:0000250}.
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_03049};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC       family. UBA4 subfamily. {ECO:0000255|HAMAP-Rule:MF_03049}.
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DR   EMBL; BC042324; AAH42324.1; -; mRNA.
DR   EMBL; BC071459; AAH71459.1; -; mRNA.
DR   RefSeq; NP_956421.1; NM_200127.1.
DR   AlphaFoldDB; Q8AWD2; -.
DR   SMR; Q8AWD2; -.
DR   STRING; 7955.ENSDARP00000013020; -.
DR   PaxDb; Q8AWD2; -.
DR   PRIDE; Q8AWD2; -.
DR   GeneID; 393095; -.
DR   KEGG; dre:393095; -.
DR   CTD; 27304; -.
DR   ZFIN; ZDB-GENE-040426-782; mocs3.
DR   eggNOG; KOG2017; Eukaryota.
DR   InParanoid; Q8AWD2; -.
DR   OrthoDB; 692426at2759; -.
DR   PhylomeDB; Q8AWD2; -.
DR   Reactome; R-DRE-947581; Molybdenum cofactor biosynthesis.
DR   UniPathway; UPA00344; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q8AWD2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016783; F:sulfurtransferase activity; ISS:UniProtKB.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; ISS:UniProtKB.
DR   GO; GO:0042292; F:URM1 activating enzyme activity; ISS:UniProtKB.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR   GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR   Gene3D; 3.40.250.10; -; 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; PTHR10953; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Disulfide bond; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW   Nucleotide-binding; Reference proteome; Transferase; tRNA processing; Zinc.
FT   CHAIN           1..459
FT                   /note="Adenylyltransferase and sulfurtransferase MOCS3"
FT                   /id="PRO_0000369195"
FT   DOMAIN          347..457
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   ACT_SITE        239
FT                   /note="Glycyl thioester intermediate; for
FT                   adenylyltransferase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   ACT_SITE        412
FT                   /note="Cysteine persulfide intermediate; for
FT                   sulfurtransferase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         120..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         181..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   DISULFID        316..324
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   CONFLICT        176
FT                   /note="V -> A (in Ref. 1; AAH71459)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="L -> P (in Ref. 1; AAH71459)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="G -> S (in Ref. 1; AAH71459)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="Y -> H (in Ref. 1; AAH71459)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  50798 MW;  BC64B05515AD9275 CRC64;
     MDDTIVSLKS QLLEREREVA TLKKKLDQIE KGNSTLPELQ EKVTSLSPLR LNTSLNNDDI
     MRYSRQLLLP ELGVKGQIAI SNISVLVVGC GGLGCPLAQY LAAAGIGRLG LLDYDVVELS
     NLHRQVLHTE LTQGQPKALS AAQAISRMNS TVQCVPYHLQ LSRENAIQLI QQYDIVADCS
     DNVPTRYLVN DACVLTSRPL VSASALRMEG QLTVYNYRGG PCYRCLYPIP PPPETVTNCS
     DGGVLGVVPG IMGCLQALEV LKIASGQECS FAQQLLMFDG EQTRFRSIRL RSRQKECVVC
     GEKPTITELQ DYEHFCGSAA TDKCRRLHLL SREQRVSVQD YKGILDHSTP HLLLDVRPKV
     EVDICRLSNS LHIPLASLED KKPEHITLLK EAISDLQEHL NNQSPVQVFV VCKLGNDSQK
     AVQLLEKMSG AEVEAMTVKD IGGGLMAWAK KIDYCFPQY
 
 
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