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

Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial (Bifunctional BIO3-BIO1 protein) [Includes: Dethiobiotin synthetase (EC 6.3.3.3) (DTB synthetase) (DTBS) (Protein BIOTIN AUXOTROPH 3); 7,8-diamino-pelargonic acid aminotransferase (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (EC 2.6.1.62) (Diaminopelargonic acid synthase) (Protein BIOTIN AUXOTROPH 1)]

 BIODA_ORYSJ             Reviewed;         821 AA.
Q6ZKV8; A0A0P0XDC2;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
30-AUG-2017, entry version 95.
RecName: Full=Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial;
AltName: Full=Bifunctional BIO3-BIO1 protein;
Includes:
RecName: Full=Dethiobiotin synthetase;
EC=6.3.3.3;
AltName: Full=DTB synthetase;
Short=DTBS;
AltName: Full=Protein BIOTIN AUXOTROPH 3;
Includes:
RecName: Full=7,8-diamino-pelargonic acid aminotransferase;
Short=DAPA AT;
Short=DAPA aminotransferase;
AltName: Full=7,8-diaminononanoate synthase;
Short=DANS;
AltName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
EC=2.6.1.62;
AltName: Full=Diaminopelargonic acid synthase;
AltName: Full=Protein BIOTIN AUXOTROPH 1;
Flags: Precursor;
Name=BIO3-BIO1; Synonyms=BIO1, BIO3;
OrderedLocusNames=Os08g0245400, LOC_Os08g14770;
ORFNames=OJ1033_B09.17, OsJ_26590;
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[2]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
-!- FUNCTION: Bifunctional enzyme that catalyzes two different
reactions involved in the biotin biosynthesis.
-!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
7,8-diaminopelargonic acid (DAPA) to form an ureido ring.
{ECO:0000250}.
-!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
(KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
animotransferase known to utilize SAM as an amino donor (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
phosphate + dethiobiotin.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 1/2.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the dethiobiotin
synthetase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-III
pyridoxal-phosphate-dependent aminotransferase family. BioA
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AP003859; BAD05190.1; -; Genomic_DNA.
EMBL; AP008214; BAF23268.1; -; Genomic_DNA.
EMBL; AP014964; BAT04525.1; -; Genomic_DNA.
EMBL; CM000145; EEE68317.1; -; Genomic_DNA.
EMBL; AK100945; BAG94844.1; -; mRNA.
RefSeq; XP_015650723.1; XM_015795237.1.
UniGene; Os.9720; -.
ProteinModelPortal; Q6ZKV8; -.
SMR; Q6ZKV8; -.
STRING; 39947.LOC_Os08g14770.1; -.
PaxDb; Q6ZKV8; -.
PRIDE; Q6ZKV8; -.
EnsemblPlants; OS08T0245400-01; OS08T0245400-01; OS08G0245400.
GeneID; 4345056; -.
Gramene; OS08T0245400-01; OS08T0245400-01; OS08G0245400.
KEGG; osa:4345056; -.
eggNOG; ENOG410IPFW; Eukaryota.
eggNOG; COG0161; LUCA.
InParanoid; Q6ZKV8; -.
KO; K19562; -.
OMA; KVEWYRG; -.
OrthoDB; EOG09360C74; -.
UniPathway; UPA00078; UER00160.
UniPathway; UPA00078; UER00161.
Proteomes; UP000059680; Chromosome 8.
Genevisible; Q6ZKV8; OS.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_00336; BioD; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR004472; DTB_synth_BioD.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53383; SSF53383; 2.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
2: Evidence at transcript level;
Aminotransferase; ATP-binding; Biotin biosynthesis; Complete proteome;
Ligase; Magnesium; Metal-binding; Mitochondrion;
Multifunctional enzyme; Nucleotide-binding; Pyridoxal phosphate;
Reference proteome; S-adenosyl-L-methionine; Transferase;
Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 821 Bifunctional dethiobiotin synthetase/7,8-
diamino-pelargonic acid aminotransferase,
mitochondrial.
/FTId=PRO_0000417697.
NP_BIND 39 44 ATP. {ECO:0000250}.
NP_BIND 194 197 ATP. {ECO:0000250}.
REGION 28 283 Dethiobiotin synthetase.
REGION 316 820 7,8-diamino-pelargonic acid
aminotransferase.
REGION 374 375 7-keto-8-aminopelargonic acid binding.
{ECO:0000250}.
REGION 436 437 Pyridoxal phosphate binding.
{ECO:0000250}.
METAL 43 43 Magnesium. {ECO:0000250}.
METAL 194 194 Magnesium. {ECO:0000250}.
BINDING 72 72 Substrate. {ECO:0000250}.
BINDING 482 482 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 626 626 Pyridoxal phosphate. {ECO:0000250}.
BINDING 655 655 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 689 689 7-keto-8-aminopelargonic acid; via
carbonyl oxygen. {ECO:0000250}.
BINDING 691 691 Pyridoxal phosphate. {ECO:0000250}.
BINDING 787 787 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
SITE 332 332 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000250}.
MOD_RES 655 655 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
SEQUENCE 821 AA; 90048 MW; 40663C38B8859EEE CRC64;
MLRLLRHARR HSTSSSSSAA AAAVPLTSPA FAVFGANTGV GKTLVSAGLV ASLLASPSPS
PSTVAYLKPL QTGFPDDSDA RFVFDRAPAL LRRLRLAGGG ASTRLVASNH TLFPSPAVDP
LPERQDTVVN YGGEEGVEEK ALVCRTVYAW REPVSPHLAA EREGMPVEDE EVRWLVDRWL
AEEDGGGEVW KVLETAGGVA SPGPSGTLQC DLYRSSRLPA VLVGDGRLGG ISSTLSAYET
LLLRGYDVGS VILEDRGLSN DRFLLSYLRK RVPVHVLPPI PEDPKDDLTD WFSESSSAFS
SLKDSLQSFH SRRVQRLNSM QRKSKYLLWW PFTQHDLVPV DSVTVIDSRF GENFSAYKVK
DKTIVPQFDA CASWWTQGPD SNLQIELARD MGYAAARYGH VMFPENVHEP ALRCAELLLG
GVGKDWASRV YFSDNGSTAI EIALKMAFRK YACDHGIIVD SEKDIRSEGS VHFKVLALNG
SYHGDTLGAM EAQAPSAYTS FLQQPWYSGR GLFLDPPTVY IKNKSANLSL PPSIMHDQLS
SCDTCFSSLT EVFCKTRDTS SAANVYVSYI SQQLSQYAMS NNSEHIAALI IEPVIQGAGG
MHLIDPLFQR LLVKECKNRK IPVIFDEVFT GFWRLGVESA SELLGCFPDI SCYAKLMTGG
IVPLAATLAT EPIFEAFRSD SKLTALLHGH SYTAHPMGCT AAVKAIQWYK DPSTNSNIDL
DRMKLKELWD SALVNHLSSL PNVKRVVSLG TLCAIELKAE GSDAGYASLY ASSLIRQLRE
EDNIYARPLG NVIYLMCGPC TTQDSCTRQL AKVHRRLQKL N


Related products :

Catalog number Product name Quantity
EIAAB28576 Homo sapiens,Human,OAT,Ornithine aminotransferase, mitochondrial,Ornithine delta-aminotransferase,Ornithine--oxo-acid aminotransferase
EIAAB28575 Bos taurus,Bovine,OAT,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
EIAAB28574 Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase,Rat,Rattus norvegicus
EIAAB28577 Mouse,Mus musculus,Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
E1612p ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Pig,Plasma membrane-associated fatty acid-binding protein,Sus 96T
U1612p CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Pig,Plasma membrane-associated fatty acid-binding protein,Sus 96T
E1612r ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Maat,mAspAT,Plasma membrane-associated fatty acid-binding protein,Ra 96T
U1612r CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Maat,mAspAT,Plasma membrane-associated fatty acid-binding protein,Rat 96T
CSB-EL002601RA Rat Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
BCAT2_HUMAN Human ELISA Kit FOR Branched-chain-amino-acid aminotransferase, mitochondrial 96T
BCAT2_MOUSE Mouse ELISA Kit FOR Branched-chain-amino-acid aminotransferase, mitochondrial 96T
E1612b ELISA kit Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid- 96T
U1612Rb CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Oryctolagus cuniculus,Plasma membrane-associated fatty acid-bi 96T
U1612m CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Got-2,mAspAT,Mouse,Mus musculus,Plasma membrane-associated fatty acid 96T
E1612Rb ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Oryctolagus cuniculus,Plasma membrane-associated fatty acid-b 96T
CSB-EL002601RA Rat Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit SpeciesRat 96T
CSB-EL002601PI Pig Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit SpeciesPig 96T
CSB-EL002601BO Bovine Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
CSB-EL002601HU Human Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
CSB-EL002601MO Mouse Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
AE54585BO Bovine Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT2) ELISA Kit 48T
EIAAB37898 Endometrial progesterone-induced protein,EPIP,Oryctolagus cuniculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,PSA,PSAT,PSAT1,Rabbit
E1612b ELISA Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid-bindi 96T
E1612h ELISA kit Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,Homo sapiens,Human,mAspAT,Plasma membrane-associated fatty acid 96T
U1612b CLIA Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid-bindin 96T


 

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