ID A0A2K3DVR8_CHLRE Unreviewed; 1447 AA.
AC A0A2K3DVR8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=CHLRE_03g152000v5 {ECO:0000313|EMBL:PNW84628.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW84628.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW84628.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
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; CM008964; PNW84628.1; -; Genomic_DNA.
DR STRING; 3055.A0A2K3DVR8; -.
DR EnsemblPlants; PNW84628; PNW84628; CHLRE_03g152000v5.
DR Gramene; PNW84628; PNW84628; CHLRE_03g152000v5.
DR InParanoid; A0A2K3DVR8; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000006906; Chromosome 3.
DR ExpressionAtlas; A0A2K3DVR8; baseline and differential.
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; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
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:UP000006906};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 1167..1382
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 679
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 446
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 1447 AA; 143783 MW; F63EF42B4D792E45 CRC64;
MGSKTSCENR EQERTQMHTG NQAHTTRHRI QSASESVSCS TKVQHSRPQD DLQGLLDSPH
EYSVELQEFR NSAGAGSYSY GGALEDIRAR EFSRLTNHAY LDYAGAALYS EAQIQACADD
LKAQLLCNPH SSSSSSPASE ALAALRRDTL ALLRADGRHY EVVITAGATA ALRLVAEAFP
WTPGASVFAH PHAVHNSVLG VRGPAAAAGA RVQLVDTQQR VGGRAGREAA AAAGADAGAD
AGADAGADAG AAAGAAAHGG VLAAEAEGAA GATAVVVEDA AGSTAAAAAA AAVAAEAPCC
YSLLALPAEC NFTGDRHPAL GEVVRHVRRH GIAGLVVGGG GSGGSGSRQT ECAAQTLNLA
AAASIRTGTS TSTDAGPMPA SRDSSPSGAP SQQSGGDSGR SNSDSDSGGG GGGRWLVLLD
AAKACATAPP DLSAVPADFV VLSYYKIFGH PTGLGALVVR REALALLGRG KSYWGGGTVE
VAVADRPFQV RRSGAAGLED GTPPFTAAAA ARHGFAFLRR LAAGGGGGGC SSHAAGTTSC
SNTSRHLPPA DATEATAVAA AVAPTGADSA VPYDGVRESL AAVHGHAVGL ARWLAARLAA
LRHSNGAPVV RLYGDWCTEL AAAVAAGRAP AAAAAAGHAD HGPTVAFNLL RADGSWVGYA
EVGRLAAMHG LHLRTGCFCN PGACGHWLRL SAEDMIRHHS SGHVCWDDHD LAEPAVGQAA
AAGEGGGSGG GSGGGSGGGV VGRVPTGAVR VSLGAVSTFA EAYAVLRLVQ RYFVQQQQQQ
QQQPQQEEQE EQVGVQQEEQ VGEVKGEQVE RQQGGEEQEA RQMPLHVPVQ EPCGGPREQP
QRPAGGQCAA GSSRADGAGR QPHLPPQGTE LGRACATAGP TQQLRPPYTL PLEALEAIAS
SCGSSSSSSS GANSSSSSTG SSSTGSSGTG SSSTGSSSTG SSGTGSSSTG SSSTGSSGTG
SSSTGSSSTG SSGRLAGILL YPVKSCAPQL VSAWPVGATG LLLDREWALV DDSGKVLTLK
QCPRMALIRP EVDLAAATLR IAPPPGAGVP PLTLRVPQLQ PPPPPLREAV AGGAAAAAGG
AADAAADAAA ADAAAAAAAT AGGPGGAVVR LDAGLVMERV QVCGDTVCTD LVDTCSAGEG
GDERVRAWFA RVLGAPCRIV QQRSGARKVR RPAGQQPKQP LAQQQQQQQQ QQAGGGAGDV
AAIGGAGGGG GGGGGGGEGS GQALVGFAND GQYLLVSQAS MDDLRRRMSP GATAAHAATS
ASAVAGGGTG GGGARPAGGS GPGELLWRLR PNLVVCGFAA YAEDNWARVR VGPLAAEVLG
SCPRCELLQV DPRAGVRRGS EVLVALAQYR RRGGRVQFGV LLAAVAGAAG PAGPAGPAAA
MDGAAEAGGA AEADGASTVA GGEGQMCKAQ AQEQEGEVGS VEWLRRRFGA GSVLVVGDVV
EACVAGA
//
