MOCOS_BOMMO
ID MOCOS_BOMMO Reviewed; 822 AA.
AC Q8IU29;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Protein maroon-like {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein organdy;
GN Name=mal {ECO:0000255|HAMAP-Rule:MF_03050}; Synonyms=og;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C108; TISSUE=Silk gland;
RX PubMed=12650690; DOI=10.1016/s0965-1748(03)00006-7;
RA Komoto N., Sezutsu H., Yukuhiro K., Banno Y., Fujii H.;
RT "Mutations of the silkworm molybdenum cofactor sulfurase gene, og, cause
RT translucent larval skin.";
RL Insect Biochem. Mol. Biol. 33:417-427(2003).
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:12650690}.
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 -!- DEVELOPMENTAL STAGE: Expressed in larvae.
CC -!- DISRUPTION PHENOTYPE: Silk moth larvae are transluscent due to the
CC absence of XDH activity and are thereby unable to synthesize uric acid.
CC {ECO:0000269|PubMed:12650690}.
CC -!- MISCELLANEOUS: Was named 'Organdy' because of the color of the
CC translucid skin.
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; AB090243; BAC22952.1; -; Genomic_DNA.
DR RefSeq; NP_001106746.1; NM_001113275.1.
DR AlphaFoldDB; Q8IU29; -.
DR SMR; Q8IU29; -.
DR GeneID; 100134930; -.
DR KEGG; bmor:100134930; -.
DR CTD; 4118; -.
DR eggNOG; KOG2142; Eukaryota.
DR InParanoid; Q8IU29; -.
DR OrthoDB; 394559at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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..822
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249955"
FT DOMAIN 658..814
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 412
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 822 AA; 94082 MW; AA5D5DC184295877 CRC64;
MTVLSQIIKP DDMIKITSEF ARLGDRCYLD NAGATLYPKS LITSINEDLL KNVYMNPHTD
KNTKDYIEQI RCLILKHFNT DPSTYTLIFT SGTTQALKLV IESFQFMKNE DDDLNCGSFV
YLEDNHTSVV GLRELAVDKD AEVVHIAHED FLNVINTKAK QTSKYTNGGN CLVAYPAQSN
FNGFKYPLNC IENIKNGCLN NHLKKHLCEI NSDWYVLLDA AAYVATSKLD LAKVQPDFVS
LSFYKIFGFP TGLGALLVKK SSENVLSQKR YFGGGTVDAL LSNEHYHIKR EIFHERFEDG
SLSFLSIISL KQCLDTMYRI IPRIIHDDIM ETISYHTFYL AKDLYCQLLD LRHRNGTKAI
KFYLDSDFSD ITKQGGVLTF NLVREDGTYI GFSEFQHMAD LFNISVRTGC FCNSGSCQRH
LHMSNKDMKD MYNAGHRCGD EVDLINEKPT GAIRISFGYY NTFEDVDKFV NMICRCFVNA
KARKQKRIIN HFVETPKIKH YNGNVNKIIN EQIYFKNVDD VLINIPPMST KIILKEICIF
PIKSCGAFKI LSGWNIGPKG FEYDREWMIV KDNGVCLTQK QNTRMCMIRP QIDLKQKVMI
LNFPGKTPIS IPLENSINEV QKNGSLCHSK VCTDMIKGID CGDEVADWIS EALEVSFLRL
IRQSSNDNRS LKKKKDEDKK LLSLSNQAQY LLINKATVKW LSEKIKDPLF TDDLNHLTDR
FRGNLIIEME QELLEREWHS VIIGNHEFKV EGQCPRCQMV CIDQQTGEKT VEPLRTIAEQ
FGGKLRFGIY LSYVGTVNKS DDRTLKTYSP IKAILNDDNI SR
