ID A0A3B0KQZ9_DROGU Unreviewed; 792 AA.
AC A0A3B0KQZ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=Ma-l {ECO:0000256|HAMAP-Rule:MF_03050};
GN Name=mal {ECO:0000256|HAMAP-Rule:MF_03050};
GN ORFNames=DGUA_6G008428 {ECO:0000313|EMBL:SPP86318.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP86318.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03050}.
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DR EMBL; OUUW01000011; SPP86318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0KQZ9; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; MOCOS_middle.
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 PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03050};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_03050}; Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 633..792
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 426
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 792 AA; 88270 MW; 80537D03BD56ABFD CRC64;
MSSYQAEYSV DEQAAIDKEF TRLANNKSIY LDHAGTTLYA ESQVAAAAEQ LQRDVICNPH
TCRLTGDYVD QVRYKVLEFF NTNEQEYHVI FTANATAGLS LVAENFDFGT SGNFHYCQEN
HTSVLGMRER VQARAIYMLK EEQISGRDAA SVASVASVNG SFKPAATLDN SLVTFSAQCN
FSGYKMPLEA IAGIQQHGLP HGPGSRISGE AGMADPSHDN NFYVCLDAAS FVATNPLDLQ
RYQPDYVCFS FYKIFGYPTG VGALLVSRRG AEAFGKRRFF GGGTINYAYP HAMDHQLREV
FHQRYEDGTL PFLSIVGLLE GFRTLERLVP RSTTDGGGGG VATMERISRH VHGLAQYLEQ
QLRELKHPNG QHLIELYNRV GYEERSRQGG IVAFNVRTDT GAFVGFGEIA CVAALQGILL
RTGCFCNIGA CQRYLRLDDA LMDGIYKRAG RICGDYFDLI DGQPTGAVRV SFGYMTRRED
VDKLLKMLRL SYLATRPQQR LQLIEEQADE LPKALKEWAQ RRPQLLQLAI YPVKSCAALK
IEGGGANWPL TAQGLQYDRE WMIVDMNGMA ITQKRCTELC LIKPHIRDDQ LVLQYGDLST
TVTLPLSLAD QAENSSRCRS KVCRQPVEGL DCGDEVAEWL SGYLGMDGLR LLRQSSRRSS
PSGEQQQQLS LVNQAQFLLV NRSSVRSLQF EESLDETVDR FRANIIIDTG TAFEELSYKQ
LTIGQVQFQV EGPCQRCDMI CINQRTGERS PDTLTTISRL QSGKMRFGIY ISRSSTANSK
EQLTCGDVVL AT
//
