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

Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)

 A0A084FWM6_9PEZI        Unreviewed;       505 AA.
A0A084FWM6;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 17.
RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
ORFNames=SAPIO_CDS9354 {ECO:0000313|EMBL:KEZ39488.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ39488.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ39488.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ39488.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
hydroxyanthranilic acid (3-OHAA), respectively.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
-!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
alanine and anthranilate from L-kynurenine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SIMILARITY: Belongs to the kynureninase family.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ39488.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; JOWA01000143; KEZ39488.1; -; Genomic_DNA.
RefSeq; XP_016639287.1; XM_016790777.1.
EnsemblFungi; KEZ39488; KEZ39488; SAPIO_CDS9354.
GeneID; 27728426; -.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_01970; Kynureninase; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR010111; Kynureninase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR14084; PTHR14084; 1.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF038800; KYNU; 1.
SUPFAM; SSF53383; SSF53383; 2.
TIGRFAMs; TIGR01814; kynureninase; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Reference proteome {ECO:0000313|Proteomes:UP000028545}.
DOMAIN 136 304 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 192 195 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_03017}.
BINDING 164 164 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03017}.
BINDING 165 165 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 276 276 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 279 279 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 301 301 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 346 346 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 374 374 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
MOD_RES 302 302 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_03017}.
SEQUENCE 505 AA; 55928 MW; B15286EE1CD5AB19 CRC64;
MEMSAFTDRL RSGKAPEFPS DANTLSFAQK LDSQDSLRHL RDEFLIPTKT SFKKKALDGT
IPGTVPLPNG TANGTHQSNG SPTADDSEKV IYFVGNSLGA QPKAVRRYID AQLETWASIG
VNGHFTDMGD SPLVAWQDMA EDCAVKSADL VGASPHEIVI MNTLTANLHM MMASFYKPTE
KRHKVILEWK PFPSDHYAIE SQIAWHGLDP AKSMVKIEPD ENCLIPTQKI LDTIDEHGDE
TALILLPGIQ YYSGQYFDMP RITAYAKAKG IVVGWDLAHA AGNVELRLHD WDVDFACWCT
YKYINAGPGS IAGAFVHERH GRVEWADDAG IDGTGRPSYR PRLMGWYGGD KRVRFNMDNK
FVPTPGAAGY QLSNPSIIDL ASLSGALSVF GKTSMHDLRS KALVLTAYAE YLMDEMQASS
PSDSEPPFRI ITPRDPAQRG TQLSVVFANS ELHDAVSASL EENGVMCDKR KPNVIRVAPV
PLYSRFEDVW RFMQILREAV RLDKA


Related products :

Catalog number Product name Quantity
201-20-3036 KYNU{kynureninase (L-kynurenine hydrolase)}rabbit.pAb 0.2ml
L1CAM KYNU Gene kynureninase (L-kynurenine hydrolase)
CSB-EL012703RA Rat kynureninase (L-kynurenine hydrolase) (KYNU) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL012703MO Mouse kynureninase (L-kynurenine hydrolase) (KYNU) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA012703GA01HU Rabbit anti-human kynureninase (L-kynurenine hydrolase) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA012703GA01HU Rabbit anti-human kynureninase (L-kynurenine hydrolase) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
30-140 Kynureninase is a pyridoxal-5'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectiv 0.1 mg
30-141 Kynureninase is a pyridoxal-5'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectiv 0.05 mg
YF-PA15999 anti-L-Kynurenine Hydrolase 50 ul
YF-MA16613 anti-L-Kynurenine Hydrolase (1G2) 100 ug
3570-15-8 nicotinic acid, compound with 2-aminoet nicotinic acid, compoun 1g
32981-34-3 nicotinic acid, compound with alpha-[(but nicotinic acid, compoun 1g
10058-07-8 nicotinic acid, compound with 3,7-dihydr nicotinic acid, compoun 1g
1748-09-0 nicotinic acid, compound with 1-[(3,4-dim nicotinic acid, compoun 1g
13602-12-5 Iso Nicotinic Acid N_Oxide Iso Nicotinic Acid N_Oxi 1g
orb84747 Mouse Kynureninase His tag protein Recombinant Mouse Kynureninase His tag protein. For research use only. 20
YF-PA16000 anti-L-Kynurenine Hydrolase type: Primary antibodies host: Rabbit 100 ul
YF-PA15999 anti-L-Kynurenine Hydrolase type: Primary antibodies host: Mouse 50 ul
EIAAB14288 AMDD,Amidase domain-containing protein,Anandamide amidohydrolase 2,FAAH2,Fatty-acid amide hydrolase 2,Homo sapiens,Human,Oleamide hydrolase 2
39658-41-8 6_Amino nicotinic acid ethyl ester 6_Amino nicotinic acid e 1g
EIAAB11760 Diphthamide biosynthesis protein 1,Diphthamide biosynthesis protein 2 homolog-like 1,Diphthamide biosynthesis protein 2-like,DPH1,DPH1 homolog,DPH2L,DPH2L1,DPH2-like 1,DPH-like 1,Homo sapiens,HsDph1,H
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-EL014703MO Mouse Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit SpeciesMouse 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
YF-MA16613 Mouse monoclonal to L-Kynurenine Hydrolase , Isotype IgG2a, Host Mouse, Clone 1G2 100 ug


 

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