MOCS3_HUMAN
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 03-AUG-2022, entry version 183.
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, AND DISULFIDE BOND.
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 ENZYME 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 ENZYME ACTIVITY, AND INTERACTION WITH NFS1.
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 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 probably acting as a sulfur donor for thiocarboxylation reactions.
CC {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332,
CC ECO:0000269|PubMed:19017811}.
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}.
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}.
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; 82.
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; O95396; -.
DR PeptideAtlas; O95396; -.
DR PRIDE; O95396; -.
DR ProteomicsDB; 50847; -.
DR Antibodypedia; 28627; 190 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 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; GTIGAMQ; -.
DR OrthoDB; 1445129at2759; -.
DR PhylomeDB; O95396; -.
DR TreeFam; TF106103; -.
DR BioCyc; MetaCyc:HS04742-MON; -.
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; 552 hits in 1093 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; IBA:GO_Central.
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; IEA:UniProtKB-EC.
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: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 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 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 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"
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 /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
