ID H0ZCU1_TAEGU Unreviewed; 1045 AA.
AC H0ZCU1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 58.
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=MOCOS {ECO:0000256|HAMAP-Rule:MF_03050,
GN ECO:0000313|Ensembl:ENSTGUP00000008402.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008402.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000008402.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000008402.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L-
CC arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine;
CC Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107;
CC Evidence={ECO:0000256|ARBA:ARBA00029322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000256|ARBA:ARBA00029322};
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 AlphaFoldDB; H0ZCU1; -.
DR STRING; 59729.ENSTGUP00000008402; -.
DR Ensembl; ENSTGUT00000008490.2; ENSTGUP00000008402.2; ENSTGUG00000008151.2.
DR GeneTree; ENSGT00940000157051; -.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; H0ZCU1; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR TreeFam; TF105761; -.
DR Proteomes; UP000007754; Chromosome 2.
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; 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; IPR011037; Pyrv_Knase-like_insert_dom_sf.
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; SSF50800; PK beta-barrel 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:UP000007754};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 868..1026
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 117..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 592
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 432
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 1045 AA; 114885 MW; C73393C088C4E340 CRC64;
MGQYPWGPAH STTLALARGT LHSFYGQESQ LDMMQEYYTP SARYEQVTSI ISSNGSGSKG
NLSLNWKILG ERDFHEEFST ACRNRRVHLL LSPANRSPGA SGKVFLTGNS SLCQRSARLS
RGRTGPGACG AGGGRGRSAG PGRAEPSGPE RSGRGGSAAA EPRCSPRRAL RARGAMAGQP
LSFRAFCAAR PAGCEYGYGH GDGLGALRDR EFPRLRGITY LDHAGSALFP ESLLKAFTDD
LRNNIYGNPH SQNISSKLTY DTIEHVRYRI LQHFHTTAED YTIIFTSGCT AALKLIAESF
PWIPEGAKQP SSRFCYLTDS HTSVIGMRGI TASMNVLSVP IKPKEILLAK SRLPAEEQNC
TTPHLFSYPA QSNFSGTKYP LSWIQDIKSG RLCPIKVPGK WFVLLDAASY VSSSPLDLGV
HQADFIPISF YKIFGFPTGL GALLVNNRIA PLLRKTYFGG GTAAAYLSGE DFYFPRKSIA
ERFEDGTVSF LDIIALKHGF DVLEKLTGGM EKIKQHTFAL AHYTYTVLSN LKYANGAPVV
RIYSDTDFSN PDVQGPIINF NVLDENGQVL GFSQVDSMAS LHNIHVRTGC FCNTGACQMH
LGISNEDIQR NLQAGHVCGD NIDLVDGRPT GSVRISFGYM SSFEDAQTFL NFIIATRLSN
LDAEIPFQSV PKRMTESVPD DHLSFNKEDK LSPILQISDR ELRNIPSEAE TTGSWQPPEP
EAESMRATVS ETAVPTCRKG GKPITVAKIY LYPIKSCSAF EVTEWPVGNQ GLLYDRNWMV
VNQNGVCMTQ KQEPRLCLVN PSIDLKQKMM LIQADGMDPI CVPLEDNTGK EAVICESKVC
SHRVKTYDCG ERIAGWLSTF LGRPCRLIRQ SSDMRSKSHQ KNTKGLSSAT NISLSLVNEA
QYLLINVASI LQLKEHISAR LKEPLEIEEL IRRFRANIVI SAPESFEEEE WAEISIGALQ
FQVVGPCSRC QIICIDQQSG ERNKEILQSL SAARGRKTNF GIYLMNQPLC SPLSDTLSVG
SEVLPVLKEN AEIKSPTSSE EKCSG
//
