ID A0A0E0Q1F9_ORYRU Unreviewed; 766 AA.
AC A0A0E0Q1F9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI06G26090.2, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI06G26090.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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|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 AlphaFoldDB; A0A0E0Q1F9; -.
DR EnsemblPlants; ORUFI06G26090.2; ORUFI06G26090.2; ORUFI06G26090.
DR Gramene; ORUFI06G26090.2; ORUFI06G26090.2; ORUFI06G26090.
DR HOGENOM; CLU_010913_0_1_1; -.
DR Proteomes; UP000008022; 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 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; 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|HAMAP-Rule:MF_03050};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 577..764
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 433
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 766 AA; 85341 MW; 470CA3A07B1AF91C 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 WFSEAIGRKG DCKQKLPVDA
MRFRPNLVIS GSSPYSEDNW KKLRIGEACF TSMGGCNRCQ MINLHQDSGQ VLKSKEPLAT
LASYRRKKGK ILFGILLNYE DIMEGENETI AGRWLQVGQQ VYPSTE
//
