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

Ketol-acid reductoisomerase (NADP( )) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase)

 V6XYT1_BIFLN            Unreviewed;       350 AA.
V6XYT1;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
25-OCT-2017, entry version 32.
RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435};
Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435};
EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435};
AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435};
Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435};
AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435};
Name=ilvC1 {ECO:0000313|EMBL:ESV32734.1};
Synonyms=ilvC {ECO:0000256|HAMAP-Rule:MF_00435};
ORFNames=BLONG_0118 {ECO:0000313|EMBL:ESV32734.1};
Bifidobacterium longum E18.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1322347 {ECO:0000313|EMBL:ESV32734.1, ECO:0000313|Proteomes:UP000018321};
[1] {ECO:0000313|Proteomes:UP000018321}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=24356845;
Zhurina D., Dudnik A., Waidmann M.S., Grimm V., Westermann C.,
Breitinger K.J., Yuan J., van Sinderen D., Riedel C.U.;
"High-Quality Draft Genome Sequence of Bifidobacterium longum E18,
Isolated from a Healthy Adult.";
Genome Announc. 1:e01084-13(2013).
-!- FUNCTION: Involved in the biosynthesis of branched-chain amino
acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
dihydroxy-isovalerate. In the isomerase reaction, S2AL is
rearranged via a Mg-dependent methyl migration to produce 3-
hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|SAAS:SAAS00905279}.
-!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
= (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
{ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00905249}.
-!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
{ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00905300}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00435};
Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00435};
-!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|SAAS:SAAS00677654}.
-!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00677656}.
-!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
{ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00677653}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CM002287; ESV32734.1; -; Genomic_DNA.
RefSeq; WP_007054663.1; NZ_CM002287.1.
ProteinModelPortal; V6XYT1; -.
EnsemblBacteria; ESV32734; ESV32734; BLONG_0118.
PATRIC; fig|1322347.4.peg.123; -.
UniPathway; UPA00047; UER00056.
UniPathway; UPA00049; UER00060.
Proteomes; UP000018321; Chromosome.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 1.10.1040.10; -; 1.
HAMAP; MF_00435; IlvC; 1.
InterPro; IPR008927; 6-PGluconate_DH_C-like.
InterPro; IPR013328; 6PGD_dom_2.
InterPro; IPR000506; AcH_isomrdctse_C.
InterPro; IPR013116; IlvN.
InterPro; IPR013023; KARI.
InterPro; IPR014359; KARI_prok.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR21371; PTHR21371; 1.
Pfam; PF01450; IlvC; 1.
Pfam; PF07991; IlvN; 1.
PIRSF; PIRSF000116; IlvC_gammaproteo; 2.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00465; ilvC; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00677648};
Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|SAAS:SAAS00677648};
Complete proteome {ECO:0000313|Proteomes:UP000018321};
Isomerase {ECO:0000313|EMBL:ESV32734.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00825999};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00825953};
NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00905200};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00825984};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00677651, ECO:0000313|EMBL:ESV32734.1}.
DOMAIN 16 179 IlvN. {ECO:0000259|Pfam:PF07991}.
DOMAIN 185 326 IlvC. {ECO:0000259|Pfam:PF01450}.
ACT_SITE 109 109 {ECO:0000256|HAMAP-Rule:MF_00435}.
METAL 192 192 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00435}.
METAL 192 192 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435}.
METAL 196 196 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00435}.
METAL 228 228 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435}.
METAL 232 232 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435}.
BINDING 49 49 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 52 52 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 54 54 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 135 135 NADP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 253 253 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00435}.
SEQUENCE 350 AA; 38566 MW; 05CA4B6A312CA639 CRC64;
MAATIWYEKD ADLSVFDGKK VAILGYGSQG HAHALNLRDS GVDVVVGLRP TSKSVEFAKE
QGLEVKPVGE AVAEADVVMI LLPDQYQAAV YKKDIEPNLK PGAALAFAHG FNIHYGYIKP
SEDHPVFMVA PKGPGHIVRR EYAAGRGVPV VVAVEQDPDG KTWPLCLAYA KALGALRAGA
IKTTFTEETE TDLFGEQDVL MGGINHLCDL GFDVLTEAGY QPEIAYFEVF HELKMLVDLA
NEGGLNKARW SCSDTAQYGD YTSTVITEET KKRMQYQLKR IQDGSFAKEF MDDQAAGAPK
FKKLQEEYSH PHLETVGPKL RAMFSWNNAE AKDKDETESF NGKIARTQVQ


Related products :

Catalog number Product name Quantity
EIAAB28640 BCKADE2,BCKAD-E2,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase co
EIAAB28639 BCATE2,BCKADE2,BCKAD-E2,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex,Dihyd
EIAAB28638 BCKADE2,BCKAD-E2,Branched-chain alpha-keto acid dehydrogenase complex component E2,Dbt,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex,Dihydrolipoa
EIAAB28645 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial,BCKDE1B,BCKDH E1-beta,Bckdhb,Branched-chain alpha-keto acid dehydrogenase E1 component beta chain,Rat,Rattus norvegicus
EIAAB28646 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial,BCKDE1B,BCKDH E1-beta,Bckdhb,Branched-chain alpha-keto acid dehydrogenase E1 component beta chain,Mouse,Mus musculus
EIAAB28648 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial,BCKDE1B,BCKDH E1-beta,BCKDHB,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
EIAAB28647 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial,BCKDE1B,BCKDH E1-beta,BCKDHB,Branched-chain alpha-keto acid dehydrogenase E1 component beta chain,Homo sapiens,Human
MC-055 BCKDH(Branched chain alpha keto acid dehydrogenase) E2 150 ug
MC-055 BCKDH(Branched chain alpha keto acid dehydrogenase) E2 150 ug
MC-056 BCKDH(Branched chain alpha keto acid dehydrogenase) kinase 100 ug
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha 5
MC-056 BCKDH(Branched chain alpha keto acid dehydrogenase) kinase 100 ug
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha 1
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha 50
REN-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha 1
MC-055 BCKDH(Branched chain alpha keto acid dehydrogenase) E2 6E12 150 ug
EIAAB28642 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,Bckdha,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Rat,Rattus norvegicus
EIAAB28644 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,Bckdha,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Mouse,Mus musculus
EIAAB28643 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,BCKDHA,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
EIAAB28641 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,BCKDHA,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Homo sapiens,Human
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1 Alpha ENZYMES 1
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha BCKDHA 1
OETENZ-090 Branched Chain keto Acid Dehydrogenase E1 Alpha Human Recombinant 1
enz-090 Recombinant Human Branched Chain keto Acid Dehydrogenase E1, Alpha BCKDHA 5
MC-056 BCKDH(Branched chain alpha keto acid dehydrogenase) kinase 12F11 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