MOCOS_NEUCR
ID MOCOS_NEUCR Reviewed; 937 AA.
AC Q7SE17; A7UW68; V5IQE9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 25-MAY-2022, entry version 100.
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};
DE AltName: Full=Nitrate nonutilizer protein 13;
GN Name=nit-13; Synonyms=hxB; ORFNames=NCU02777, NCU21396;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP GENE NAME.
RX PubMed=6449399; DOI=10.1093/genetics/95.3.649;
RA Tomsett A.B., Garrett R.H.;
RT "The isolation and characterization of mutants defective in nitrate
RT assimilation in Neurospora crassa.";
RL Genetics 95:649-660(1980).
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}.
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DR EMBL; CM002236; ESA44393.1; -; Genomic_DNA.
DR RefSeq; XP_011393025.1; XM_011394723.1.
DR AlphaFoldDB; Q7SE17; -.
DR SMR; Q7SE17; -.
DR STRING; 5141.EFNCRP00000002451; -.
DR EnsemblFungi; ESA44393; ESA44393; NCU02777.
DR GeneID; 3880421; -.
DR KEGG; ncr:NCU02777; -.
DR VEuPathDB; FungiDB:NCU02777; -.
DR HOGENOM; CLU_010913_0_0_1; -.
DR InParanoid; Q7SE17; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..937
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000423953"
FT DOMAIN 682..935
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 633..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
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"
SQ SEQUENCE 937 AA; 102078 MW; EA9F2895BD5D26BC CRC64;
MGSLNIQHNG YDADVEKIRE EEYPMLKDSI YLDHAGTTPY PKSLMDRFAQ EMTTNLFGNP
HSASASSQLS TQRIQDIRLR ALQFFNADPA DFDLVFVANA TAGIKLVVEA MRCLPTGFDY
VYHQSSHTSL VGVREEARSS VCLDTRQVED WLSGSCPFDD NEDEERPILF AYPAQSNMDG
RRFPLSWSSQ ICRQSLSPTN KRKTYTLLDA AALVSSSPLD LSNAETAPDF VVLSFYKIFG
FPDLGALIVR KEVQDVFLSR RYFGGGTVDM VVCLKEQWHA PKDGFLHERL EDGTLPIHSI
IALDVAMDVH AKLFGSMERV AGHTGFLARR LYQGLKGLRH ANDELVCAIY SPDPETEESG
PLVAFNIRNA QGIWISLAEV EKLATLKGIH IRTGGVCNPG GIASALGLEP WEMKQNFSSG
FRCGTDNDTM GGKPTGIIRV SLGAMSTIAD VDRFVQFVKE FYCEDTPPIL PPPETKLDPS
LRNTPELFIK SIVVYPIKSC AGFHVPPGID WEVRPEGLVW DREWCLVHRG SGQALSQKRY
PRMALLRPNL DFTKGELQVT FAGDISSSPG LPSSISVPLS KNPKMYAPKK SGMSSRVCGE
EITPQTYASA QINDFFSTVL GVPCVLARFP PGGQGKGMTR HAKAHLQRHQ HQQPHPAVSV
STRLTKPAMM PGAFPSPKAV ETPPSPPDSD TERSATPTQE AQGPKPRRIL LSNESPILAI
TSTSVDALNQ SIALLNPSVS QPISEAVFRA NLVLSPSPST PSASPSNPLT PSPSPSTTSK
PTPKPKQKPK QKLNPYEEDT WSSLTIFNSS SFSSSSSSCS TPSSSGFQTT TKFQMLGSCR
RCHMVCIDQT TGSKTAGGEP FVTLSKTRRF EGKVFFGVHM GLQAEDEEDG HAEDIEKEGT
GMGMGTGTGT GTGTRSMGGN GSVVKVRVGD VVRPSYL
