MOCOS_ASPTN
ID MOCOS_ASPTN Reviewed; 828 AA.
AC Q0CLW8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN Name=hxB {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=ATEG_05316;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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:0000255|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: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 -!- 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; CH476600; EAU34385.1; -; Genomic_DNA.
DR RefSeq; XP_001214494.1; XM_001214494.1.
DR AlphaFoldDB; Q0CLW8; -.
DR SMR; Q0CLW8; -.
DR STRING; 341663.Q0CLW8; -.
DR EnsemblFungi; EAU34385; EAU34385; ATEG_05316.
DR GeneID; 4321216; -.
DR VEuPathDB; FungiDB:ATEG_05316; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR Proteomes; UP000007963; 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; 3.40.640.10; -; 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 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..828
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369381"
FT DOMAIN 652..825
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 638..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 828 AA; 91321 MW; 752809D440122372 CRC64;
MTEAIINEGS PLGYSQGYSE DIDAIRQREY PMLSDTTYLD HAGTTLYAKS LIDSFSRDLT
TNLFGNPHSL SASSQRTTQR VDDIRLRALR FFNADPEHFD LVFVANATSA IKLVADALRD
SAHGFWYGYH VDAHTSLVGA RELAQAGSRC FTTDEEVEAW IAQLDADRTG AAQLFAFPAQ
SNMNGRRLPL RWCGRIRDRT KETATTYTLL DAASLVATSP LDLSDVSAAS DFTVLSFYKI
FGFPDLGALI VRKSAGHIFA QRRFFGGGTV DMVLTQDTQW HAKKRSVHEI LEDGTLPFHN
IIALDSALDT HARLYGSMGN VSTHTRFLAR TLYDRLAALR HFNGERVVHF YMGRSPDFAD
ASAQGPILAF NLRSSQGGWI GKSEVERLAS VKSLQIRSGT LCNPGGTASQ LGWSGADMLR
HFSAGLRCGD DHDVMDGRPT GILRVSLGAM SNLRDVEAFV AFVEEFYVEK TPNVCSVVPS
AADDSLQAGF YVESLAVYPI KSCGAFKVPD GQRWEIRREG LAWDREWCLV HQGTGAALNQ
KRYPRMALIR PHIDLARGVL RVVCGEASSE QKTLEISLRR EDASLVTTSL CQNAAKPSTV
CGDQVVVQVY SSTAVSSFFS TFLDVPCTLA RFPPQSTTRY TRRSLHSRSS TAALRRQRPV
EESSMPGSFP SDTPLSRTPE PPPILLANES PILLISRSSV NRLNETIKAS AKKAVAADVF
RANIVVAENL PHQLANTERP YIEDRWESFT VGPDRLQFDV LGSCQRCQMV CIDQCSGERR
DEPFSTLAKT RKVGSQIVFG RHAAVADGVD GISRTVMVGD VVRPWYPE
