Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Molybdenum cofactor sulfurase (MCS) (MOS) (MoCo sulfurase) (EC 2.8.1.9) (Abscisic acid protein 3) (Low expression of osmotically expressive genes protein 5) (Molybdenum cofactor sulfurtransferase)

 MOCOS_ARATH             Reviewed;         819 AA.
Q9C5X8; Q9FX72;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 100.
RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:11553608, ECO:0000269|PubMed:15561708};
AltName: Full=Abscisic acid protein 3;
AltName: Full=Low expression of osmotically expressive genes protein 5;
AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
Name=ABA3; Synonyms=LOS5; OrderedLocusNames=At1g16540;
ORFNames=F19K19.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF GLY-469.
PubMed=11553608; DOI=10.1074/jbc.C100472200;
Bittner F., Oreb M., Mendel R.R.;
"ABA3 is a molybdenum cofactor sulfurase required for activation of
aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana.";
J. Biol. Chem. 276:40381-40384(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
AND MUTAGENESIS OF GLY-106 AND GLY-469.
PubMed=11549764; DOI=10.1105/tpc.13.9.2063;
Xiong L., Ishitani M., Lee H., Zhu J.-K.;
"The arabidopsis los5/aba3 locus encodes a molybdenum cofactor
sulfurase and modulates cold stress- and osmotic stress-responsive
gene expression.";
Plant Cell 13:2063-2083(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=14726515; DOI=10.1074/jbc.M312929200;
Hesberg C., Haensch R., Mendel R.R., Bittner F.;
"Tandem orientation of duplicated xanthine dehydrogenase genes from
Arabidopsis thaliana: differential gene expression and enzyme
activities.";
J. Biol. Chem. 279:13547-13554(2004).
[6]
COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
PYRIDOXAL PHOSPHATE AT LYS-271, AND MUTAGENESIS OF LYS-271 AND
CYS-430.
PubMed=15561708; DOI=10.1074/jbc.M411195200;
Heidenreich T., Wollers S., Mendel R.R., Bittner F.;
"Characterization of the NifS-like domain of ABA3 from Arabidopsis
thaliana provides insight into the mechanism of molybdenum cofactor
sulfuration.";
J. Biol. Chem. 280:4213-4218(2005).
[7]
FUNCTION OF C-TERMINAL DOMAIN.
PubMed=18258600; DOI=10.1074/jbc.M708549200;
Wollers S., Heidenreich T., Zarepour M., Zachmann D., Kraft C.,
Zhao Y., Mendel R.R., Bittner F.;
"Binding of sulfurated molybdenum cofactor to the C-terminal domain of
ABA3 from Arabidopsis thaliana provides insight into the mechanism of
molybdenum cofactor sulfuration.";
J. Biol. Chem. 283:9642-9650(2008).
-!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of
molybdenum is essential for xanthine dehydrogenase (XDH) and
aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is
liganded by 1 oxygen and 1 sulfur atom in active form. Modulates
cold stress- and osmotic stress-responsive gene expression by
acting as key regulator of abscisic acid (ABA) biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:11549764,
ECO:0000269|PubMed:11553608, ECO:0000269|PubMed:14726515,
ECO:0000269|PubMed:15561708, ECO:0000269|PubMed:18258600}.
-!- CATALYTIC ACTIVITY: Molybdenum cofactor + L-cysteine + reduced
acceptor + 2 H(+) = thio-molybdenum cofactor + L-alanine + H(2)O +
oxidized acceptor. {ECO:0000255|HAMAP-Rule:MF_03050,
ECO:0000269|PubMed:11553608, ECO:0000269|PubMed:15561708}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000255|HAMAP-Rule:MF_03050,
ECO:0000269|PubMed:15561708};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for L-cysteine {ECO:0000269|PubMed:15561708};
KM=200 uM for L-selenocysteine {ECO:0000269|PubMed:15561708};
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11549764}.
-!- INDUCTION: Up-regulated in response to drought, salt or ABA
treatment. {ECO:0000269|PubMed:11549764}.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
Rule:MF_03050}.
-!- SEQUENCE CAUTION:
Sequence=AAG10824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF325457; AAK12939.1; -; mRNA.
EMBL; AY034895; AAK58888.1; -; mRNA.
EMBL; AC011808; AAG10824.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE29467.1; -; Genomic_DNA.
PIR; G86300; G86300.
RefSeq; NP_564001.1; NM_101519.3.
UniGene; At.18927; -.
ProteinModelPortal; Q9C5X8; -.
STRING; 3702.AT1G16540.1; -.
iPTMnet; Q9C5X8; -.
PaxDb; Q9C5X8; -.
PRIDE; Q9C5X8; -.
EnsemblPlants; AT1G16540.1; AT1G16540.1; AT1G16540.
GeneID; 838224; -.
Gramene; AT1G16540.1; AT1G16540.1; AT1G16540.
KEGG; ath:AT1G16540; -.
Araport; AT1G16540; -.
TAIR; locus:2017943; AT1G16540.
eggNOG; KOG2142; Eukaryota.
eggNOG; COG0520; LUCA.
eggNOG; COG3217; LUCA.
HOGENOM; HOG000029698; -.
InParanoid; Q9C5X8; -.
KO; K15631; -.
OMA; RVNTYDC; -.
OrthoDB; EOG093603XR; -.
PhylomeDB; Q9C5X8; -.
BRENDA; 2.8.1.9; 399.
Reactome; R-ATH-947581; Molybdenum cofactor biosynthesis.
PRO; PR:Q9C5X8; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C5X8; baseline and differential.
Genevisible; Q9C5X8; AT.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IDA:TAIR.
GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009000; F:selenocysteine lyase activity; IDA:TAIR.
GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IDA:TAIR.
GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
GO; GO:0009409; P:response to cold; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0010118; P:stomatal movement; IMP:TAIR.
GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_03050; MOCOS; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR005302; MoCF_Sase_C.
InterPro; IPR028886; MoCo_sulfurase.
InterPro; IPR005303; MOSC_N.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
Pfam; PF00266; Aminotran_5; 2.
Pfam; PF03473; MOSC; 1.
Pfam; PF03476; MOSC_N; 1.
SUPFAM; SSF50800; SSF50800; 1.
SUPFAM; SSF53383; SSF53383; 2.
PROSITE; PS51340; MOSC; 1.
1: Evidence at protein level;
Complete proteome; Molybdenum cofactor biosynthesis;
Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 819 Molybdenum cofactor sulfurase.
/FTId=PRO_0000249958.
DOMAIN 650 817 MOSC. {ECO:0000255|HAMAP-Rule:MF_03050}.
ACT_SITE 430 430
MOD_RES 271 271 N6-(pyridoxal phosphate)lysine.
MUTAGEN 106 106 G->E: In los5-1; induces a deficience in
stress-induced ABA accumulation.
{ECO:0000269|PubMed:11549764}.
MUTAGEN 271 271 K->S: Loss of function.
{ECO:0000269|PubMed:15561708}.
MUTAGEN 430 430 C->A: Induces a strong reduction in
enzyme activity.
{ECO:0000269|PubMed:15561708}.
MUTAGEN 469 469 G->E: In aba3-1; induces a reduced ABA
biosynthesis.
{ECO:0000269|PubMed:11549764,
ECO:0000269|PubMed:11553608}.
SEQUENCE 819 AA; 91803 MW; 81FE806B186B4007 CRC64;
MEAFLKEFGD YYGYPDGPKN IQEIRDTEFK RLDKGVVYLD HAGSTLYSEL QMEYIFKDFT
SNVFGNPHSQ SDISSATSDL IADARHQVLE YFNASPEDYS CLFTSGATAA LKLVGETFPW
TQDSNFLYTM ENHNSVLGIR EYALAQGASA CAVDIEEAAN QPGQLTNSGP SIKVKHRAVQ
MRNTSKLQKE ESRGNAYNLF AFPSECNFSG LRFNLDLVKL MKENTETVLQ GSPFSKSKRW
MVLIDAAKGC ATLPPDLSEY PADFVVLSFY KLFGYPTGLG ALLVRNDAAK LLKKTYFSGG
TVAASIADID FVKRRERVEE FFEDGSASFL SIAAIRHGFK LLKSLTPSAI WMHTTSLSIY
VKKKLQALRH GNGAAVCVLY GSENLELSSH KSGPTVTFNL KRPDGSWFGY LEVEKLASLS
GIQLRTGCFC NPGACAKYLE LSHSELRSNV EAGHICWDDN DVINGKPTGA VRVSFGYMST
FEDAKKFIDF IISSFASPPK KTGNGTVVSG RFPQLPSEDL ESKESFPSHY LKSITVYPIK
SCAGFSVIRW PLCRTGLLHD REWMVQGLTG EILTQKKVPE MSLIKTFIDL EEGLLSVESS
RCEDKLHIRI KSDSYNPRND EFDSHANILE NRNEETRINR WFTNAIGRQC KLLRYSSSTS
KDCLNRNKSP GLCRDLESNI NFANEAQFLL ISEESVADLN RRLEAKDEDY KRAHEKLNPH
RFRPNLVISG GEPYGEDKWK TVKIGDNHFT SLGGCNRCQM INISNEAGLV KKSNEPLTTL
ASYRRVKGKI LFGTLLRYEI DEKRQCWIGV GEEVNPDIE


Related products :

Catalog number Product name Quantity
EIAAB25085 MCS,MoCo sulfurase,Mocos,Molybdenum cofactor sulfurase,MOS,Mouse,Mus musculus
EIAAB25086 Bos taurus,Bovine,MCS,MCSU,MoCo sulfurase,MOCOS,Molybdenum cofactor sulfurase,MOS
EIAAB25084 hMCS,Homo sapiens,Human,MCS,MoCo sulfurase,MOCOS,Molybdenum cofactor sulfurase,MOS
EH1514 Molybdenum cofactor sulfurase Elisa Kit 96T
201-20-3430 MOCOS{molybdenum cofactor sulfurase}rabbit.pAb 0.2ml
MOCS2 MOCOS Gene molybdenum cofactor sulfurase
E13459h Human Molybdenum Cofactor Sulfurase ELISA Kit 96T
CSB-EL014702HU Human Molybdenum cofactor sulfurase(MOCOS) ELISA kit 96T
CSB-EL014702MO Mouse Molybdenum cofactor sulfurase(MOCOS) ELISA kit 96T
CSB-EL014702BO Bovine Molybdenum cofactor sulfurase(MOCOS) ELISA kit 96T
CSB-EL014702BO Bovine Molybdenum cofactor sulfurase(MOCOS) ELISA kit SpeciesBovine 96T
CSB-EL014702MO Mouse Molybdenum cofactor sulfurase(MOCOS) ELISA kit SpeciesMouse 96T
CSB-EL014702HU Human Molybdenum cofactor sulfurase(MOCOS) ELISA kit SpeciesHuman 96T
MOCOS_MOUSE ELISA Kit FOR Molybdenum cofactor sulfurase; organism: Mouse; gene name: Mocos 96T
CSB-EL014703HU Human Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit SpeciesHuman 96T
CSB-EL014703BO Bovine Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit SpeciesBovine 96T
CSB-EL014703MO Mouse Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit SpeciesMouse 96T
CSB-EL014703HU Human Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
CSB-EL014703MO Mouse Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
CSB-EL014703BO Bovine Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
EIAAB25089 Cell migration-inducing gene 11 protein,Homo sapiens,Human,MIG11,MOCS1,Molybdenum cofactor biosynthesis protein 1,Molybdenum cofactor synthesis-step 1 protein A-B
CSB-EL014702MO Mouse molybdenum cofactor sulfurase (MOCOS) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL014702BO Bovine molybdenum cofactor sulfurase (MOCOS) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL014702HU Human molybdenum cofactor sulfurase (MOCOS) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB25080 Mocs2,MOCS2B,Molybdenum cofactor synthesis protein 2 large subunit,Molybdenum cofactor synthesis protein 2B,Molybdopterin synthase catalytic subunit,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur