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

4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)

 F4AQ60_GLAS4            Unreviewed;       267 AA.
F4AQ60;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 50.
RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018068};
Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018030};
Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
OrderedLocusNames=Glaag_2046 {ECO:0000313|EMBL:AEE22991.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE22991.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE22991.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE22991.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
{ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00011094}.
-!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6-
dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-
tetrahydrodipicolinate + NAD(P)H. {ECO:0000256|HAMAP-
Rule:MF_00102, ECO:0000256|SAAS:SAAS00018108}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
{ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018087}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018118}.
-!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|HAMAP-
Rule:MF_00102, ECO:0000256|SAAS:SAAS00671951}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- CAUTION: Was originally thought to be a dihydrodipicolinate
reductase (DHDPR), catalyzing the conversion of
dihydrodipicolinate to tetrahydrodipicolinate. However, it was
shown in E.coli that the substrate of the enzymatic reaction is
not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
the DapA-catalyzed reaction. {ECO:0000256|HAMAP-Rule:MF_00102}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP002526; AEE22991.1; -; Genomic_DNA.
RefSeq; WP_007988072.1; NC_015497.1.
STRING; 983545.Glaag_2046; -.
EnsemblBacteria; AEE22991; AEE22991; Glaag_2046.
KEGG; gag:Glaag_2046; -.
eggNOG; ENOG4105DUK; Bacteria.
eggNOG; COG0289; LUCA.
KO; K00215; -.
OrthoDB; POG091H01P6; -.
UniPathway; UPA00034; UER00018.
Proteomes; UP000006544; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
HAMAP; MF_00102; DapB; 1.
InterPro; IPR022663; DapB_C.
InterPro; IPR000846; DapB_N.
InterPro; IPR022664; DapB_N_CS.
InterPro; IPR023940; DHDPR_bac.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR20836; PTHR20836; 1.
Pfam; PF05173; DapB_C; 1.
Pfam; PF01113; DapB_N; 1.
PIRSF; PIRSF000161; DHPR; 1.
SUPFAM; SSF51735; SSF51735; 2.
TIGRFAMs; TIGR00036; dapB; 1.
PROSITE; PS01298; DAPB; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018109};
Complete proteome {ECO:0000313|Proteomes:UP000006544};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018059};
Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018031};
Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018109};
NAD {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018069};
NADP {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00484099};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00484120, ECO:0000313|EMBL:AEE22991.1}.
DOMAIN 3 125 DapB_N. {ECO:0000259|Pfam:PF01113}.
DOMAIN 128 264 DapB_C. {ECO:0000259|Pfam:PF05173}.
NP_BIND 8 13 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
NP_BIND 98 100 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
NP_BIND 122 125 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
REGION 165 166 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00102}.
ACT_SITE 155 155 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00102}.
ACT_SITE 159 159 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00102}.
BINDING 35 35 NADP. {ECO:0000256|HAMAP-Rule:MF_00102}.
BINDING 156 156 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00102}.
SEQUENCE 267 AA; 28304 MW; 7B70DF3B5D88C7CF CRC64;
MNKIAIFGAN GRMGRVLIDA LDQAQNATLC AAYVRASSSM MGVDVGELAG IGQRGLTVSD
ANSGDFKQTD ILIDFTLPEA LEANLALCVT HNKPIVIGTT GLNQQQKEAL QQASQHIPIV
FAANYSVGVN LLLNLARQTA RVMGDTADIE IIEGHHRFKK DAPSGTAVAI GEAIADELGR
DLATCAVYGR EGDTGERDQK TIGFATVRAG DIVGEHTTLF ADIGERIELT HKASSRLTFA
KGAVKAAVWL KDKPAGLYDM QDVLGLA


Related products :

Catalog number Product name Quantity
EIAAB10691 Carbonyl reductase II,DCXR,Dicarbonyl_L-xylulose reductase,Homo sapiens,Human,kiDCR,Kidney dicarbonyl reductase,L-xylulose reductase,Sperm surface protein P34H,XR
EIAAB11124 7-dehydrocholesterol reductase,7-DHC reductase,D7SR,DHCR7,Homo sapiens,Human,Putative sterol reductase SR-2,Sterol Delta(7)-reductase
EIAAB11127 7-dehydrocholesterol reductase,7-DHC reductase,Dhcr7,Rat,Rattus norvegicus,Sterol Delta(7)-reductase
EIAAB11126 7-dehydrocholesterol reductase,7-DHC reductase,Bos taurus,Bovine,DHCR7,Sterol Delta(7)-reductase
EIAAB11125 7-dehydrocholesterol reductase,7-DHC reductase,Dhcr7,Mouse,Mus musculus,Sterol Delta(7)-reductase
E2220h AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human
U2220h CLIA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
U2220h CLIA kit AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
E2220h ELISA kit AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
E2220h ELISA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
EIAAB13217 ANG1,Another new gene 1 protein,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Homo sapiens,Human,Putative sterol reductase SR-1,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily m
EIAAB05625 3-oxoacyl-[acyl-carrier-protein] reductase,Bos taurus,Bovine,Carbonyl reductase family member 4,CBR4,Quinone reductase CBR4
EIAAB05628 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Quinone reductase CBR4,Rat,Rattus norvegicus
EIAAB05627 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Mouse,Mus musculus,Quinone reductase CBR4
EIAAB05626 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,CBR4,Homo sapiens,Human,Quinone reductase CBR4
EIAAB11121 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,Dhcr24,Kiaa0018,Mouse,Mus musculus
EIAAB11123 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,DHCR24,Diminuto_dwarf1 homolog,Homo sapiens,Human,KIAA0018,Seladin-1
EIAAB11122 24-dehydrocholesterol reductase,3-beta-hydroxysterol delta-24-reductase,Delta(24)-sterol reductase,Dhcr24,Rat,Rattus norvegicus
EIAAB25528 Homo sapiens,Human,Mitochondrial peptide methionine sulfoxide reductase,MSRA,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase
EIAAB27759 Azoreductase,DTD,DT-diaphorase,Menadione reductase,NAD(P)H dehydrogenase [quinone] 1,NAD(P)H quinone oxidoreductase 1,Nmor1,Nqo1,Phylloquinone reductase,QR1,Quinone reductase 1,Rat,Rattus norvegicus
EIAAB27760 Azoreductase,DIA4,DTD,DT-diaphorase,Homo sapiens,Human,Menadione reductase,NAD(P)H dehydrogenase [quinone] 1,NAD(P)H quinone oxidoreductase 1,NMOR1,NQO1,Phylloquinone reductase,QR1,Quinone reductase 1
EIAAB25530 Mitochondrial peptide methionine sulfoxide reductase,Mouse,Msra,Mus musculus,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase
EIAAB25529 Mitochondrial peptide methionine sulfoxide reductase,Msra,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase,Rat,Rattus norvegicus
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
EIAAB44153 Homo sapiens,Human,TGR,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,TRXR3,TXNRD3


 

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