ID   MOCS3_HUMAN             Reviewed;         460 AA.
AC   O95396;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-NOV-2023, entry version 190.
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   AltName: Full=Molybdopterin synthase sulfurylase;
DE            Short=MPT synthase sulfurylase;
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, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
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, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
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 {ECO:0000255|HAMAP-Rule:MF_03049};
GN   Synonyms=UBA4 {ECO:0000255|HAMAP-Rule:MF_03049};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   FUNCTION IN BIOSYNTHESIS OF THE MOLYBDENUM COFACTOR, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-239; CYS-316; CYS-324; CYS-365 AND CYS-412.
RX   PubMed=15073332; DOI=10.1073/pnas.0308191101;
RA   Matthies A., Rajagopalan K.V., Mendel R.R., Leimkuehler S.;
RT   "Evidence for the physiological role of a rhodanese-like protein for the
RT   biosynthesis of the molybdenum cofactor in humans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5946-5951(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACTIVE SITE, DISULFIDE BOND, AND SULFHYDRATION AT CYS-412.
RX   PubMed=15910006; DOI=10.1021/bi0503448;
RA   Matthies A., Nimtz M., Leimkuehler S.;
RT   "Molybdenum cofactor biosynthesis in humans: identification of a persulfide
RT   group in the rhodanese-like domain of MOCS3 by mass spectrometry.";
RL   Biochemistry 44:7912-7920(2005).
RN   [5]
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-413; LEU-414; GLY-415; ASN-416;
RP   ASP-417; PRO-458 AND TYR-460.
RX   PubMed=17459099; DOI=10.1111/j.1742-4658.2007.05811.x;
RA   Krepinsky K., Leimkuehler S.;
RT   "Site-directed mutagenesis of the active site loop of the rhodanese-like
RT   domain of the human molybdopterin synthase sulfurase MOCS3. Major
RT   differences in substrate specificity between eukaryotic and bacterial
RT   homologs.";
RL   FEBS J. 274:2778-2787(2007).
RN   [6]
RP   CATALYTIC ACTIVITY, INTERACTION WITH NFS1, ACTIVE SITE, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND SULFHYDRATION AT CYS-412.
RX   PubMed=18650437; DOI=10.1074/jbc.m804064200;
RA   Marelja Z., Stoecklein W., Nimtz M., Leimkuehler S.;
RT   "A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor
RT   for MOCS3, a protein involved in molybdenum cofactor biosynthesis.";
RL   J. Biol. Chem. 283:25178-25185(2008).
RN   [7]
RP   FUNCTION IN 2-THIOLATION OF TRNA.
RX   PubMed=19017811; DOI=10.1073/pnas.0808756105;
RA   Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E., Ploegh H.L.;
RT   "A functional proteomics approach links the ubiquitin-related modifier Urm1
RT   to a tRNA modification pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH NFS1.
RX   PubMed=23593335; DOI=10.1371/journal.pone.0060869;
RA   Marelja Z., Mullick Chowdhury M., Dosche C., Hille C., Baumann O.,
RA   Loehmannsroeben H.G., Leimkuehler S.;
RT   "The L-cysteine desulfurase NFS1 is localized in the cytosol where it
RT   provides the sulfur for molybdenum cofactor biosynthesis in humans.";
RL   PLoS ONE 8:e60869-e60869(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=30817134; DOI=10.1021/acs.biochem.8b01160;
RA   Neukranz Y., Kotter A., Beilschmidt L., Marelja Z., Helm M., Graef R.,
RA   Leimkuehler S.;
RT   "Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent
RT   Localization of NFS1 at the Tips of the Centrosome.";
RL   Biochemistry 58:1786-1798(2019).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 335-460.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the human MOCS3 rhodanese-like domain.";
RL   Submitted (JUL-2009) to the PDB data bank.
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 acting as a sulfur donor for thiocarboxylation reactions.
CC       {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332,
CC       ECO:0000269|PubMed:19017811, ECO:0000269|PubMed:30817134}.
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, ECO:0000269|PubMed:15073332,
CC         ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
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, ECO:0000269|PubMed:15073332,
CC         ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.25 mM for thiosulfate {ECO:0000269|PubMed:15073332};
CC         KM=0.28 mM for cyanide {ECO:0000269|PubMed:15073332};
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   -!- SUBUNIT: Interacts with NFS1. {ECO:0000255|HAMAP-Rule:MF_03049,
CC       ECO:0000269|PubMed:18650437, ECO:0000269|PubMed:23593335}.
CC   -!- INTERACTION:
CC       O95396; P54253: ATXN1; NbExp=6; IntAct=EBI-373206, EBI-930964;
CC       O95396; Q13148: TARDBP; NbExp=3; IntAct=EBI-373206, EBI-372899;
CC       O95396; Q9BTM9: URM1; NbExp=4; IntAct=EBI-373206, EBI-714589;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049,
CC       ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:23593335}.
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; AF102544; AAC72412.1; -; mRNA.
DR   EMBL; AL034553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015939; AAH15939.1; -; mRNA.
DR   CCDS; CCDS13435.1; -.
DR   RefSeq; NP_055299.1; NM_014484.4.
DR   PDB; 3I2V; X-ray; 1.25 A; A=335-460.
DR   PDBsum; 3I2V; -.
DR   AlphaFoldDB; O95396; -.
DR   SMR; O95396; -.
DR   BioGRID; 118127; 91.
DR   DIP; DIP-31168N; -.
DR   IntAct; O95396; 16.
DR   STRING; 9606.ENSP00000244051; -.
DR   ChEMBL; CHEMBL4295684; -.
DR   iPTMnet; O95396; -.
DR   PhosphoSitePlus; O95396; -.
DR   BioMuta; MOCS3; -.
DR   EPD; O95396; -.
DR   jPOST; O95396; -.
DR   MassIVE; O95396; -.
DR   MaxQB; O95396; -.
DR   PaxDb; 9606-ENSP00000244051; -.
DR   PeptideAtlas; O95396; -.
DR   ProteomicsDB; 50847; -.
DR   Pumba; O95396; -.
DR   Antibodypedia; 28627; 204 antibodies from 24 providers.
DR   DNASU; 27304; -.
DR   Ensembl; ENST00000244051.3; ENSP00000244051.1; ENSG00000124217.5.
DR   GeneID; 27304; -.
DR   KEGG; hsa:27304; -.
DR   MANE-Select; ENST00000244051.3; ENSP00000244051.1; NM_014484.5; NP_055299.1.
DR   UCSC; uc002xvy.3; human.
DR   AGR; HGNC:15765; -.
DR   CTD; 27304; -.
DR   GeneCards; MOCS3; -.
DR   GeneReviews; MOCS3; -.
DR   HGNC; HGNC:15765; MOCS3.
DR   HPA; ENSG00000124217; Low tissue specificity.
DR   MIM; 609277; gene.
DR   neXtProt; NX_O95396; -.
DR   OpenTargets; ENSG00000124217; -.
DR   PharmGKB; PA30904; -.
DR   VEuPathDB; HostDB:ENSG00000124217; -.
DR   eggNOG; KOG2017; Eukaryota.
DR   GeneTree; ENSGT00940000160847; -.
DR   HOGENOM; CLU_013325_1_2_1; -.
DR   InParanoid; O95396; -.
DR   OMA; MIYDALE; -.
DR   OrthoDB; 53913at2759; -.
DR   PhylomeDB; O95396; -.
DR   TreeFam; TF106103; -.
DR   BioCyc; MetaCyc:HS04742-MONOMER; -.
DR   BRENDA; 2.7.7.80; 2681.
DR   BRENDA; 2.8.1.11; 2681.
DR   PathwayCommons; O95396; -.
DR   Reactome; R-HSA-947581; Molybdenum cofactor biosynthesis.
DR   SABIO-RK; O95396; -.
DR   SignaLink; O95396; -.
DR   UniPathway; UPA00344; -.
DR   UniPathway; UPA00988; -.
DR   BioGRID-ORCS; 27304; 588 hits in 1184 CRISPR screens.
DR   ChiTaRS; MOCS3; human.
DR   EvolutionaryTrace; O95396; -.
DR   GeneWiki; MOCS3; -.
DR   GenomeRNAi; 27304; -.
DR   Pharos; O95396; Tbio.
DR   PRO; PR:O95396; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; O95396; Protein.
DR   Bgee; ENSG00000124217; Expressed in sperm and 114 other tissues.
DR   Genevisible; O95396; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA: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; IDA:FlyBase.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016783; F:sulfurtransferase activity; IDA:UniProtKB.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IMP:UniProtKB.
DR   GO; GO:0042292; F:URM1 activating enzyme activity; IDA:UniProtKB.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0043545; P:molybdopterin cofactor metabolic process; IDA:UniProtKB.
DR   GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR   GO; GO:0034227; P:tRNA thio-modification; IDA:UniProtKB.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB.
DR   CDD; cd01526; RHOD_ThiF; 1.
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   1: Evidence at protein level;
KW   3D-structure; 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..460
FT                   /note="Adenylyltransferase and sulfurtransferase MOCS3"
FT                   /id="PRO_0000120583"
FT   DOMAIN          347..458
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT   REGION          158..238
FT                   /note="Interaction with NFS1"
FT                   /evidence="ECO:0000269|PubMed:23593335"
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                   ECO:0000269|PubMed:15910006, ECO:0000269|PubMed:18650437"
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   MOD_RES         412
FT                   /note="Cysteine persulfide"
FT                   /evidence="ECO:0000269|PubMed:15910006,
FT                   ECO:0000269|PubMed:18650437"
FT   DISULFID        316..324
FT                   /evidence="ECO:0000269|PubMed:15910006"
FT   VARIANT         429
FT                   /note="S -> A (in dbSNP:rs7269297)"
FT                   /id="VAR_049349"
FT   MUTAGEN         239
FT                   /note="C->A: Impairs sulfurtransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15073332"
FT   MUTAGEN         316
FT                   /note="C->A: Does not affect sulfurtransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15073332"
FT   MUTAGEN         324
FT                   /note="C->A: Does not affect sulfurtransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15073332"
FT   MUTAGEN         365
FT                   /note="C->A: Does not affect sulfurtransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15073332"
FT   MUTAGEN         412
FT                   /note="C->A: Abolishes sulfurtransferase activity."
FT                   /evidence="ECO:0000269|PubMed:15073332"
FT   MUTAGEN         413
FT                   /note="K->R: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         414
FT                   /note="L->K: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         415
FT                   /note="G->A: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         416
FT                   /note="N->V: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         417
FT                   /note="D->R: Results in 470-fold increased activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         417
FT                   /note="D->T: Results in 90-fold increased activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         458
FT                   /note="P->G: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   MUTAGEN         460
FT                   /note="Y->A: Does not affect sulfurtransferase specificity
FT                   and activity."
FT                   /evidence="ECO:0000269|PubMed:17459099"
FT   HELIX           338..347
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          352..355
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   HELIX           359..364
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   HELIX           375..379
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   HELIX           383..397
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          406..411
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          413..416
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   HELIX           417..430
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   STRAND          437..442
FT                   /evidence="ECO:0007829|PDB:3I2V"
FT   HELIX           445..452
FT                   /evidence="ECO:0007829|PDB:3I2V"
SQ   SEQUENCE   460 AA;  49669 MW;  299A4E755173E324 CRC64;
     MASREEVLAL QAEVAQREEE LNSLKQKLAS ALLAEQEPQP ERLVPVSPLP PKAALSRDEI
     LRYSRQLVLP ELGVHGQLRL GTACVLIVGC GGLGCPLAQY LAAAGVGRLG LVDYDVVEMS
     NLARQVLHGE ALAGQAKAFS AAASLRRLNS AVECVPYTQA LTPATALDLV RRYDVVADCS
     DNVPTRYLVN DACVLAGRPL VSASALRFEG QITVYHYDGG PCYRCIFPQP PPAETVTNCA
     DGGVLGVVTG VLGCLQALEV LKIAAGLGPS YSGSLLLFDA LRGHFRSIRL RSRRLDCAAC
     GERPTVTDLL DYEAFCGSSA TDKCRSLQLL SPEERVSVTD YKRLLDSGAF HLLLDVRPQV
     EVDICRLPHA LHIPLKHLER RDAESLKLLK EAIWEEKQGT QEGAAVPIYV ICKLGNDSQK
     AVKILQSLSA AQELDPLTVR DVVGGLMAWA AKIDGTFPQY
//