ID E4UNR8_ARTGP Unreviewed; 841 AA.
AC E4UNR8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
GN Name=hxB {ECO:0000256|HAMAP-Rule:MF_03050};
GN ORFNames=MGYG_02684 {ECO:0000313|EMBL:EFQ99671.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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; DS989823; EFQ99671.1; -; Genomic_DNA.
DR RefSeq; XP_003175154.1; XM_003175106.1.
DR AlphaFoldDB; E4UNR8; -.
DR STRING; 535722.E4UNR8; -.
DR GeneID; 10030460; -.
DR VEuPathDB; FungiDB:MGYG_02684; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR InParanoid; E4UNR8; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000002669; 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; 1.
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:UP000002669};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 667..839
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 841 AA; 92792 MW; 9AEFC2EE4BC26B15 CRC64;
MVSIEDSPSY YKKPVEKIRA DQYPLLKDTT YLDHAGTTLY AKSLIESFSQ RLTSNLFGNP
HSASSSSQLS TSIIDDARLR VLRFCNASPE DFDVVFVANA TAGIKLVAES LRDNEPEGFW
YGYHVDSHTS LVGVRNMADL GSRCLVTDHE VTSWINQLHN DYNKPESPCL TLFAYPGQSN
MTGRRLPLSW CKEVRACIGK DRKWRAFTLF DAASLASTSP LDLSDTACAP DFTVVSFYKI
FGFPDLGALI VRKDAGHLFQ NRKYFGGGTV GMVLAVGEQW HAKKDSTLHD QLEDGTLPFH
NIVALHSAFD VHERLYTSMD NISRHTAEMA RILYDGLSSL EHGNGAKVCQ IYKGPGGYAE
RTLQGPIISF NLKDSTGRWI KKSDVERLAA VKNIQIRSGT LCNPGGMAYY LGLKPGDMKR
NYNAGQRCGD DNDIIAGKPT GGLRVSLGAM TSKQDINTFL DFIRNFYVEN CIISEPKPQK
GTLNPAIQPS PSHFYIEKLC IYPIKSCGAF TIPGSTEWNV KPEGLAWDRE WCLIHQGTGS
ALNQKRYPRM ALIRPVIDLP RSTLRVTLPS PGPHGDTMEI PLSVDSTDLA EGQLCRNFTK
QQSTVCGDTV SVQVYKSARL ASFFSDFLGV PCTLARFPPQ QHHSAARFSK SYRNPIKELV
HNPNAVDKIP GAFPEPIASG TRRPILLSNE GPILIISRSS VNNVNESIKS SGKPNSASRT
VAADVFRANI IVCEKAAAPA ADLVPAYRPS AVCEQPYIEE LWTGFQVGDA HFDALGSCQR
CQMICIDQHT ATRSDEPFST LAKTRKVDGK VYFGKHVCLS NKSEDKPITI KTGGLLIPFY
N
//
