ID   MOCOS_ORYSJ             Reviewed;         824 AA.
AC   Q655R6; B9FQF2; Q0DA83; Q0MRQ5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 110.
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 sulfurase-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN   Name=MCSU3; OrderedLocusNames=Os06g0670000, LOC_Os06g45860;
GN   ORFNames=OsJ_22313 {ECO:0000312|EMBL:EEE66194.1}, P0686E06.35;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang S.-J., Huang P.-M.;
RT   "Characterization of the rice molybdenum cofactor sulfurase family genes.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   -!- 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   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03050}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD45451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF20240.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; DQ855409; ABH88164.1; -; mRNA.
DR   EMBL; AP003635; BAD45451.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008212; BAF20240.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014962; BAS99067.1; -; Genomic_DNA.
DR   EMBL; CM000143; EEE66194.1; -; Genomic_DNA.
DR   RefSeq; XP_015644048.1; XM_015788562.1.
DR   AlphaFoldDB; Q655R6; -.
DR   SMR; Q655R6; -.
DR   STRING; 4530.OS06T0670000-01; -.
DR   PaxDb; Q655R6; -.
DR   PRIDE; Q655R6; -.
DR   EnsemblPlants; Os06t0670000-01; Os06t0670000-01; Os06g0670000.
DR   GeneID; 4341801; -.
DR   Gramene; Os06t0670000-01; Os06t0670000-01; Os06g0670000.
DR   KEGG; osa:4341801; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_1_1; -.
DR   InParanoid; Q655R6; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000007752; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q655R6; OS.
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   GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   Pfam; PF00266; Aminotran_5; 2.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF50800; SSF50800; 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..824
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000249960"
FT   DOMAIN          655..822
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   CONFLICT        183
FT                   /note="R -> K (in Ref. 1; ABH88164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="A -> V (in Ref. 1; ABH88164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        722
FT                   /note="R -> H (in Ref. 1; ABH88164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        799..800
FT                   /note="DI -> GT (in Ref. 1; ABH88164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   824 AA;  91836 MW;  C596481F44D8289A CRC64;
     MEVSKEEFLR QFGGDYGYPG APKGVDEMRA AEFKRLEGMA YLDHAGATLY SEAQMADVLK
     DLASNVYGNP HSQSDSSMAA SDLVTAARHQ VLKYFNASPR EYKCIFTSGA TAALKLVGEC
     FPWSRESCYM YTMENHNSVL GIREYALSKG ATVLAVDVEE GADLAKDNGS YSLYKISRRT
     NQRRSKDVLS HNCQNGSLSD ISGNNWNIFA FPSECNFSGQ KFSLSLVKLI KEGKIPLQQQ
     GKWMVLIDAA KGCATEPPNL TVYPADFVVC SFYKIFGYPT GLGALIVKNE AANLLNKTYF
     SGGTVAASIA DIDFVQKRKN IEQVLEDGTI SFLNIASLRH GFKIIEMLTT SAIERHTTSL
     ATYVRNKMLD LKHSNEINVC TIYGQQYSKV EGLKMGPTIT FNLKREDGSW FGYREVEKLA
     SLFGIHLRTG CFCNPGACAK YLGLSHSDLV SNFEAGHVCW DDNDIINGKP TGAVRISFGY
     MSTFEDAEKF LKFLQSSFVS LPVQFNNGYM LNLNSLNLID NSSQKAVSDI HLKSIIIYPV
     KSCQGFSVKS WPLTTGGLMY DREWLLQGSG GEILTQKKVP ELGSIRTLID LELGKLFIES
     PTRRDKLQLS LLESLADLSE EVDVFGQRYE VQSYDDRVNT WFSEAIGRPC TLVRCSSSKY
     RSCTYTGLRD RPCRDTQSKL NFVNEGQLLL ISEESISDLN SRLNSGKGDC KQKLPVDAMR
     FRPNLVISGS SPYSEDNWKK LRIGEACFTS MGGCNRCQMI NLHQDSGQVL KSKEPLATLA
     SYRRKKGKIL FGILLNYEDI MEGENETIAG RWLQVGQQVY PSTE