ID MOCOS_DICDI Reviewed; 1007 AA.
AC Q559G8; Q8T2S7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 27-MAR-2024, entry version 109.
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=mocos; ORFNames=DDB_G0272935;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000008; EAL71105.2; -; Genomic_DNA.
DR RefSeq; XP_644848.2; XM_639756.2.
DR AlphaFoldDB; Q559G8; -.
DR SMR; Q559G8; -.
DR STRING; 44689.Q559G8; -.
DR PaxDb; 44689-DDB0252757; -.
DR EnsemblProtists; EAL71105; EAL71105; DDB_G0272935.
DR GeneID; 8618529; -.
DR KEGG; ddi:DDB_G0272935; -.
DR dictyBase; DDB_G0272935; mocos.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q559G8; -.
DR OMA; PCTRCQM; -.
DR PhylomeDB; Q559G8; -.
DR Reactome; R-DDI-947581; Molybdenum cofactor biosynthesis.
DR PRO; PR:Q559G8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:dictyBase.
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:dictyBase.
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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..1007
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000331264"
FT DOMAIN 816..995
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 33..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 359
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 1007 AA; 114389 MW; EE20F7F7FFBBA597 CRC64;
MLIFIISIII TIASIIFLFE TVFNKNSNTI NNNNNSNNNN NNNNNNNNNN NNNKNNIKEN
NIDKNKEIKI KEKLILNNND PKENDLKYKE EFNNFLNKFS KNQEYGYKDN LIDNELRNHY
NNNNNNNNNN NNNNKDDQFP KLKDIVYLDH AASTLASMNQ IEEISKELKN SMFCNPHSVN
PIGLKTKEEV DSIRENILNY FNAPYRQYSV IFTSGCTDSL KKVGEYFAWT KNSKFYYSLE
SHNSLLGIRE YACESIGGSS TTSFQPIPSL YFKCNNNQFN DILEIIGNND DNNNESYSLF
GYPGQCNYSG TKYPLELINR IQKKYPKCKV LLDAASLVST SSFDLTKYPV DFMTISFYKM
FGYPTGIGAL IVKNDSGEKC LINKKYFSGG TVNVSMAQER FHVDRPSLSE RLEDGTINFM
NIISLKHGFN IINNQLGGID NVKLHTFSLT QYCKEEMLKL YHSDNSKQQQ LCIIYSDNHF
KDSSKQGSII NFNIFRSNGE LFGYNQVEKL ASLSSIYLRT GCFCNPGACH GYLNLSKKDI
EQHLKDGHVC WDSKDILNGK PTGSVRISFG YMNNFNDVYK FINFLKSNFI NDHKFEKEVI
KSNKKINNNL CDISDNISCS GSCGGSCGSS GSGIEDYQVQ YSNNIKEEKE EEEKEEIENL
KNEKDNDEVL LSEIYIYPVK SCSGHKVVND KWELVPSGLK YDREWTIIDQ SGNYINQKKL
PILALIQTEI DLINDKLILT APEMKVLSIP LSYYPISAFD QIQVCGDKVD GLLYGDKDFS
NTSGSSAGSG GGGGGNIDNI SEWLYQFIGK RCYLVRKSPE SHRKSKVDSS NEISFANESP
YLLINEESVS DLKKRIIKDN PDSVPSDWNW ISKHSFRANF IITGGKAYQE DLWSQFQLIS
KQQNDTTQSS SSPLVFNSVG DCNRCKMICI NQKMGIEERE PLSTLASYRR SGGKIIFGQH
LNFADSIKRN NSHTNDTALS SNESSISSSN PIFLHVPSKL KVLSERY
//
