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

Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase)

 A0A2E6VCQ1_9FLAO        Unreviewed;       215 AA.
A0A2E6VCQ1;
31-JAN-2018, integrated into UniProtKB/TrEMBL.
31-JAN-2018, sequence version 1.
25-APR-2018, entry version 4.
RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
EC=1.4.3.5 {ECO:0000256|HAMAP-Rule:MF_01629};
AltName: Full=PNP/PMP oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
Short=PNPOx {ECO:0000256|HAMAP-Rule:MF_01629};
AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01629};
Name=pdxH {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000313|EMBL:MBL86786.1};
ORFNames=CMO82_09045 {ECO:0000313|EMBL:MBL86786.1};
Winogradskyella sp.
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Winogradskyella.
NCBI_TaxID=1883156 {ECO:0000313|EMBL:MBL86786.1};
[1] {ECO:0000313|EMBL:MBL86786.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SP247 {ECO:0000313|EMBL:MBL86786.1};
Tully B.J., Graham E.D., Heidelberg J.F.;
"The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from
the Global Oceans.";
Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
5'-phosphate (PLP). {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987863}.
-!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000256|HAMAP-
Rule:MF_01629, ECO:0000256|SAAS:SAAS00987855}.
-!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
phosphate + H(2)O(2). {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987911}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2};
Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2};
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS00987914}.
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS00987916}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987977}.
-!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
family. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987851}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01629}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:MBL86786.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; PBLD01000007; MBL86786.1; -; Genomic_DNA.
UniPathway; UPA01068; UER00304.
UniPathway; UPA01068; UER00305.
GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-UniRule.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 2.30.110.10; -; 1.
HAMAP; MF_01629; PdxH; 1.
InterPro; IPR000659; Pyridox_Oxase.
InterPro; IPR019740; Pyridox_Oxase_CS.
InterPro; IPR011576; Pyridox_Oxase_put.
InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
InterPro; IPR012349; Split_barrel_FMN-bd.
PANTHER; PTHR10851:SF0; PTHR10851:SF0; 1.
Pfam; PF10590; PNP_phzG_C; 1.
Pfam; PF01243; Putative_PNPOx; 1.
PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
TIGRFAMs; TIGR00558; pdxH; 1.
PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2, ECO:0000256|SAAS:SAAS00987981};
FMN {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|PIRSR:PIRSR000190-2,
ECO:0000256|SAAS:SAAS00987981};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987970};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00987912}.
DOMAIN 43 119 Putative_PNPOx.
{ECO:0000259|Pfam:PF01243}.
DOMAIN 174 215 PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
NP_BIND 63 68 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
NP_BIND 78 79 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
NP_BIND 142 143 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
REGION 9 12 Substrate binding.
{ECO:0000256|PIRSR:PIRSR000190-1}.
REGION 193 195 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-1}.
COILED 142 169 {ECO:0000256|SAM:Coils}.
BINDING 68 68 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-1}.
BINDING 85 85 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 107 107 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 125 125 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-1}.
BINDING 129 129 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-1}.
BINDING 133 133 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-1}.
BINDING 187 187 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 197 197 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
SEQUENCE 215 AA; 25191 MW; 165DF3C151B4EA4B CRC64;
MEKDLSNYRK SYEKGELLLS NVSDNPIELF RDWFVEVDNH FNIDEANAMT ISTIGLDGYP
KSRVVLLKKY TFEGFVFYTN YNSEKGKAIE ANPNVCLSFF WHAAERQVII KGKAERIAEN
MSDGYFESRP RGSQLGAIVS NQSEVIKNRA VLEEELKALE LAYEGKDIER PKYWGGYIVR
PVEMEFWQGR PNRLHDRIRY KLLEDYNWKI ERLSP


Related products :

Catalog number Product name Quantity
EIAAB31717 Homo sapiens,Human,PNPO,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
EIAAB31718 Bos taurus,Bovine,PNPO,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
EIAAB31719 Pnpo,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase,Rat,Rattus norvegicus
EIAAB31720 Mouse,Mus musculus,Pnpo,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 20
REN-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
PNRC1 PNPO Gene pyridoxamine 5'-phosphate oxidase
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 1mg
7-03395 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 20
7-03396 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 5
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 20
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 5
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 100
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 20
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 20
OETENZ-030 Pyridoxamine 5'-Phosphate Oxidase Human Recombinant 5
7-03394 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
201-20-4333 PNPO{pyridoxamine 5'-phosphate oxidase}rabbit.pAb 0.2ml
OETENZ-030 Pyridoxamine 5'-Phosphate Oxidase Human Recombinant 20
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 5
RAN-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase MONOCLONAL ANTIBODIES 5


 

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