ID   MOCOS_SOLLC             Reviewed;         816 AA.
AC   Q8LGM7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE            EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN   Name=FLACCA;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12164810; DOI=10.1046/j.1365-313x.2002.01363.x;
RA   Sagi M., Scazzocchio C., Fluhr R.;
RT   "The absence of molybdenum cofactor sulfuration is the primary cause of the
RT   flacca phenotype in tomato plants.";
RL   Plant J. 31:305-317(2002).
CC   -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC       is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC       (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC       1 sulfur atom in active form. {ECO:0000255|HAMAP-Rule:MF_03050,
CC       ECO:0000269|PubMed:12164810}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC         thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:12164810}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03050}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY074788; AAL71858.1; -; mRNA.
DR   RefSeq; NP_001234144.1; NM_001247215.1.
DR   AlphaFoldDB; Q8LGM7; -.
DR   SMR; Q8LGM7; -.
DR   STRING; 4081.Solyc07g066480.2.1; -.
DR   PaxDb; Q8LGM7; -.
DR   PRIDE; Q8LGM7; -.
DR   EnsemblPlants; Solyc07g066480.3.1; Solyc07g066480.3.1; Solyc07g066480.3.
DR   GeneID; 543832; -.
DR   Gramene; Solyc07g066480.3.1; Solyc07g066480.3.1; Solyc07g066480.3.
DR   KEGG; sly:543832; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_1_1; -.
DR   InParanoid; Q8LGM7; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   PhylomeDB; Q8LGM7; -.
DR   Proteomes; UP000004994; Chromosome 7.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_03050; MOCOS; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR028886; MoCo_sulfurase.
DR   InterPro; IPR005303; MOSC_N.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 2.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   2: Evidence at transcript level;
KW   Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..816
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000249959"
FT   DOMAIN          647..812
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   816 AA;  91161 MW;  6C2C3E01770E56D6 CRC64;
     MNIESEKEQF LKEFGSYYGY ANSPKNIDEI RATEFKRLND TVYLDHAGAT LYSESQMEAV
     FKDLNSTLYG NPHSQSTCSL ATEDIVGKAR QQVLSFFNAS PREYSCIFTS GATAALKLVG
     ETFPWSSNSS FMYSMENHNS VLGIREYALS KGAAAFAVDI EDTHVGESES PQSNLKLTQH
     HIQRRNEGGV LKEGMTGNTY NLFAFPSECN FSGRKFDPNL IKIIKEGSER ILESSQYSRG
     CWLVLIDAAK GCATNPPNLS MFKADFVVFS FYKLFGYPTG LGALIVRKDA AKLMKKTYFS
     GGTVTAAIAD VDFFKRREGV EEFFEDGTIS FLSITAIQHG FKIINMLTTS SIFRHTTSIA
     AYVRNKLLAL KHENGEFVCT LYGLLSSEMG PTVSFNMKRP DGTWYGYREV EKLATLAGIQ
     LRTGCFCNPG ACAKYLGLSH LDLLSNIEAG HVCWDDRDIL HGKPTGAVRV SFGYMSTFED
     AMKFVNFVES NFVISSFNRC ALQPRSISLP IEGIAEAAAR HFLTSITVYP IKSCAGFSVD
     QWPLTSTGLL HDREWILKST TGEILTQKKV PEMCYISTLI DLNLGKLFVE SPRCKEKLQI
     ELKSSSLVTE RDEMDIQNHR YEVTSYNNEV DIWFSRAIDR PCTLLRNSDS QSHSCINKNG
     SPGMCRDVGA RLNFVNEAQF LLISEESIKD LNSRLKSNGR RRNGGQAVQV GVMRFRPNLV
     ASSGEPYAED GWSNINIGGK YFMSLGGCNR CQMININPEA GEVQRFTEPL ATLAGYRRAK
     GKIMFGILLR YENNTKTESD TWIRVGEEII PNGDRH