ID A0A151WES0_9HYME Unreviewed; 824 AA.
AC A0A151WES0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ALC60_14729 {ECO:0000313|EMBL:KYQ46307.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ46307.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ46307.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ46307.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ46307.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ983238; KYQ46307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WES0; -.
DR STRING; 64791.A0A151WES0; -.
DR Proteomes; UP000075809; 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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 678..824
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 824 AA; 93824 MW; D1229EB1B6B9F9BB CRC64;
MDTIVEFTPV YDDATVRSLA NEFSRLKGEC YVDHAGATLY SDTQIRNVGA DLHGSLYANP
HSIGSSLTQD IIERTRYRVL SHFNTNPDEY SVIFTSGATA SLKIIAEGFR FITNENKIAT
SPHSGSFVYV QDNHTSVLGM RDVVAARGAD VICLGHDQAF QVLSQHSTTT HDFNERRNSN
SLFVYSAQCN FSGLKYPLKW INDAHAGALS VFAKKPSTRW YVLLDAASFV ATNKLDLSIY
KPDFVCLSFY KMFGYPTGIG VLLVKNKNSD VLDKIYYGGG SVDIALSSER FHRKRQILYQ
RFEDGTVPFL SIASLQYGFE ILSKLTMDQI SKHVFSLAKT LHHSLLTLHH CNDKPVVKLY
SDSDYEDRRS QGGIVTFNVM RSNGEYVGYM EVLNMAAIFK IHLRTGCFCN PGACQRHLSL
STKDILQNYE TGYTCSGTAD LINGKPTGAV RISFGYMSTI KDVQTILLMI TKCFIDKPCI
RKFPEWWKDH KMGIFKNHKN FYNSNIDYSV SRIIKNEKNV NNFQNNFHNE NKNLDHIRNS
INFNKINTQI NKYILQRLFI YPIKSCGAYE ITDSWNLNSK GLEYDREWMI MTSSGTCLTQ
KHYTNLCLLK PVIVKKQKIM RLTYPGMPMI EISLENTYEK SIKHPICQSR ICESRVEGID
CGSEVSEWLS LALGKPNLRL VRQSHGRQKK GLDKTELSFS SQAQYLAINE ASVSWLIDKI
SHDLDFKEDT AMHRFRGNII VEGCEAFDEI KWEHIRIGNN NFKVNGPCTR CQMICIDQTT
GKKTIEPLRT LAEKFHGKLK FGIYLTRLEN TQSMLKIGDH IYCS
//
