ID C1GXZ2_PARBA Unreviewed; 887 AA.
AC C1GXZ2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=PAAG_03275 {ECO:0000313|EMBL:EEH41712.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH41712.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH41712.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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 EMBL; KN293999; EEH41712.1; -; Genomic_DNA.
DR RefSeq; XP_002794730.1; XM_002794684.1.
DR AlphaFoldDB; C1GXZ2; -.
DR STRING; 502779.C1GXZ2; -.
DR GeneID; 9097901; -.
DR KEGG; pbl:PAAG_03275; -.
DR VEuPathDB; FungiDB:PAAG_03275; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:UP000002059};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 696..882
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 671..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 887 AA; 98151 MW; 740158166B0A3118 CRC64;
MGFLHISPRT DIIMKPQLLH GEQDGKTGGN GLRGSYTDDI ETIREREYPC LKGTTYLDHA
GTTLYPISLI DAFSREMTTN LFGNPHSASS SSQLSTRRVD DARIRVLQFF NASPDHFDVV
FVANATAGIK LVADALRDCD ECGFWYGYHV DAHTSLVGVR ELAARGRRCF VDDNEVEDWI
SDQHSSIMRR PPQGPTLFAY PAQSNMTGRR LPLDWCRKLR VCNNSNKTRN IYTLLDAASL
VSTSPLDLSD PESAPDFTTL SFYKVFGFPD LGALIVRKAS GHIFNKRRYF GGGTVGMVTS
LENQWHAKKS TSIHDQLEDG TLPFHSIIAL HSAVDVHQRI YGSMENISRH TGALAKLLYD
RLSSKRHANG TLVCEMYKHQ ESSYEDRTTQ GPIVSFNMKN SKGEWVGKSE VEKLAAVKGI
QIRSGTLCNP GGMAYHLGLK VEEMKRNYNA GQRCGDDNDI IGGKPTGGLR VSLGAMSSIG
DVNKFLDFIE VFYVDKSNND APSVSLGFAQ GEGFPTSRFF VDRLCVYPIK SCGAFTIPKG
KQWEIKPEGL AWDREWCLVH QGTGVALSLK KYPRMALIRP VIDLERGVLR ISRGMLGTDP
HCLELPLLRD SDDITTRELC ENSVKKSSTV CGDQVIVQIY SSPVVSAFFS DFLEVPCTLA
RFPANSSIRY SKPQPRYQKS SETSPLSINM PGAFPHTTSS PTVSSPLHKN PILLSNESPI
LLISRSSVNR LNETIKSSGK YTSTGTKAVA ADVFRANIIV AENPVAVHQS GNSNNGVPTS
TPTLSAEHPY IEDAWTGFRI RGHKFDILGS CQRCQMVCVD QFTAVRSEEP FSTLAKTRRF
NGKVMFGRHV CLSPSVAEVH EGMGMDEGER VMIQTGDVLE PFYNETL
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