ID   MOCOS_EMENI             Reviewed;         839 AA.
AC   Q9UV64; C8VNI3; Q5BCU3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 105.
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=hxB {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=AN1637;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11029694; DOI=10.1046/j.1365-2958.2000.02119.x;
RA   Amrani L., Primus J., Glatigny A., Arcangeli L., Scazzocchio C.,
RA   Finnerty V.;
RT   "Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila
RT   melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a
RT   mechanism for the insertion of the terminal sulphur atom in the
RT   molybdopterin cofactor.";
RL   Mol. Microbiol. 38:114-125(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   INDUCTION.
RX   PubMed=10096075; DOI=10.1046/j.1365-2958.1999.01242.x;
RA   Amrani L., Cecchetto G., Scazzocchio C., Glatigny A.;
RT   "The hxB gene, necessary for the post-translational activation of purine
RT   hydroxylases in Aspergillus nidulans, is independently controlled by the
RT   purine utilization and the nicotinate utilization transcriptional
RT   activating systems.";
RL   Mol. Microbiol. 31:1065-1073(1999).
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:11029694}.
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   -!- INDUCTION: By the nicotinate utilization transcriptional activating
CC       systems. {ECO:0000269|PubMed:10096075}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03050}.
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DR   EMBL; AF128114; AAF22564.1; -; Genomic_DNA.
DR   EMBL; AACD01000026; EAA64757.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85269.1; -; Genomic_DNA.
DR   RefSeq; XP_659241.1; XM_654149.1.
DR   AlphaFoldDB; Q9UV64; -.
DR   SMR; Q9UV64; -.
DR   STRING; 162425.CADANIAP00008275; -.
DR   EnsemblFungi; CBF85269; CBF85269; ANIA_01637.
DR   EnsemblFungi; EAA64757; EAA64757; AN1637.2.
DR   GeneID; 2875359; -.
DR   KEGG; ani:AN1637.2; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_0_1; -.
DR   InParanoid; Q9UV64; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IBA:GO_Central.
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:0043545; P:molybdopterin cofactor metabolic process; IBA:GO_Central.
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   Pfam; PF00266; Aminotran_5; 1.
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..839
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000249963"
FT   DOMAIN          656..834
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   REGION          651..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   CONFLICT        78..82
FT                   /note="VDDIR -> AGRYS (in Ref. 1; AAF22564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="T -> S (in Ref. 1; AAF22564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   839 AA;  92527 MW;  0D3C8DFAE34CA1B6 CRC64;
     MNLSKGTAAA YCSGYSEDVD VIREREYPLL KDTTYLDHAG TTLYANSLIH SFGRDLTGNL
     YGNPHSMSAS SQLSAQRVDD IRLRALRFFN ADPDEFDLVF VANATAGIKL VADALQNSPQ
     GFWYGYYVDA HTSLVGVREL AKMGSRCFVN EDEVDSWISG LGSRREESLG LFAYPAQSNM
     NGRRVPMRWC EQIRAQKENA DNMIYTLLDA ASFVSTSPLD LSKIAAAPDF TVLSFYKIFG
     FPDLGALIVR KSSGDVFKHR KFFGGGTVDM VLTDGNPWHA KKQSSIHQSL EDGTLPFHSI
     IALDSAFETH GRLFRSMENV ASHTRFLAKR LRDRMNALKH YNGTKVCQLY MSPNSSYDDA
     SSQGPILAFN LRNSRGMWIG KSEVERLASI KNIQIRSGTL CNPGGTALSL GWTGADMLRH
     FSAGMRCGDD HDIMDERPTG ILRISLGAMS SLTDVDTFIA FLEEFYVDKP PEGLPVPLTG
     NVSLHQPSFY VESLSVYPIK SCGAFRIPDG QRWEVRREGL AWDREWCLVH QGTGITLNQK
     RYPRMALIRP TLDLERCLLR ITCGEANSRD GKTLEISLNR IGTNSLTTSL CQNASKPSTV
     CGDKVVLQAY TSPAVSRFFT DFLGVPCTLA RFPPQSSTRF HSRATAAINR DQNYSQKQSP
     SMPGSFPQAP SSPDPYPTPI LLSNESPLLL ISRSSVNRLN ESIKSASQPC SNPGSAASKK
     AVAADVFRAN VVVAENISTA ERPYIEDTWA SLSIGSGPEQ LRFDVLGSCE RCQMVCVDQY
     TGQRGDEPYA TLAKTRKIDR KILFGRHISP VGRPKDAENG CLGTIMVGDA VTPSYDNES