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

Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase)

 A0A074JZ98_9RHOB        Unreviewed;       224 AA.
A0A074JZ98;
01-OCT-2014, integrated into UniProtKB/TrEMBL.
01-OCT-2014, sequence version 1.
28-MAR-2018, entry version 27.
RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914410};
Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
Name=adk {ECO:0000256|HAMAP-Rule:MF_00235};
ORFNames=DT23_11790 {ECO:0000313|EMBL:KEO60893.1};
Thioclava indica.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Thioclava.
NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60893.1, ECO:0000313|Proteomes:UP000027471};
[1] {ECO:0000313|EMBL:KEO60893.1, ECO:0000313|Proteomes:UP000027471}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60893.1,
ECO:0000313|Proteomes:UP000027471};
PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
"Thioclava indica sp. nov., isolated from surface seawater of the
Indian Ocean.";
Antonie Van Leeuwenhoek 107:297-304(2015).
-!- FUNCTION: Catalyzes the reversible transfer of the terminal
phosphate group between ATP and AMP. Plays an important role in
cellular energy homeostasis and in adenine nucleotide metabolism.
{ECO:0000256|HAMAP-Rule:MF_00235}.
-!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
Rule:MF_00235, ECO:0000256|RuleBase:RU003331,
ECO:0000256|SAAS:SAAS00763738}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|SAAS:SAAS00914379}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914390}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331}.
-!- DOMAIN: Consists of three domains, a large central CORE domain and
two small peripheral domains, NMPbind and LID, which undergo
movements during catalysis. The LID domain closes over the site of
phosphoryl transfer upon ATP binding. Assembling and dissambling
the active center during each catalytic cycle provides an
effective means to prevent ATP hydrolysis. Some bacteria have
evolved a zinc-coordinating structure that stabilizes the LID
domain. {ECO:0000256|HAMAP-Rule:MF_00235}.
-!- SIMILARITY: Belongs to the adenylate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEO60893.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AUNB01000013; KEO60893.1; -; Genomic_DNA.
EnsemblBacteria; KEO60893; KEO60893; DT23_11790.
UniPathway; UPA00588; UER00649.
Proteomes; UP000027471; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
CDD; cd01428; ADK; 1.
HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
InterPro; IPR006259; Adenyl_kin_sub.
InterPro; IPR000850; Adenylat/UMP-CMP_kin.
InterPro; IPR033690; Adenylat_kinase_CS.
InterPro; IPR007862; Adenylate_kinase_lid-dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR23359; PTHR23359; 1.
Pfam; PF05191; ADK_lid; 1.
PRINTS; PR00094; ADENYLTKNASE.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01351; adk; 1.
PROSITE; PS00113; ADENYLATE_KINASE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000027471};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:KEO60893.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00235};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|SAAS:SAAS00914406};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Reference proteome {ECO:0000313|Proteomes:UP000027471};
Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:KEO60893.1};
Zinc {ECO:0000256|HAMAP-Rule:MF_00235}.
DOMAIN 133 169 ADK_lid. {ECO:0000259|Pfam:PF05191}.
NP_BIND 16 21 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
NP_BIND 63 65 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
NP_BIND 91 94 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
REGION 36 65 NMPbind. {ECO:0000256|HAMAP-
Rule:MF_00235}.
COILED 165 185 {ECO:0000256|SAM:Coils}.
METAL 136 136 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 139 139 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 156 156 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 159 159 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
BINDING 37 37 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 42 42 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 98 98 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 133 133 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 167 167 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 178 178 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 206 206 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00235}.
SEQUENCE 224 AA; 23564 MW; D54178E86CB495DF CRC64;
MTDAKSAVLI LLGPPGAGKG TQARMLEDKF GLVQLSTGDL LRAAVAEGTP AGKAAKAVME
EGGLVSDEIV LAILRDRLAQ PDVARGIILD GFPRTAGQAA DLDKLLHHTG QNVNAAISLE
VDDEAMITRV AGRYTCAKCG EGYHDEFKQP EVAGVCDKCG GTDFKRRADD NAETARARLE
AYHAQTAPLI AHYRALGVLQ EIDAMGSIDK IAADLGSVVQ RVSA


Related products :

Catalog number Product name Quantity
18-003-44255 Adenylate kinase isoenzyme 4. mitochondrial - EC 2.7.4.3; Adenylate kinase 3-like 1; ATP-AMP transphosphorylase Polyclonal 0.1 mg Protein A
29-573 AK3L1 is a member of the adenylate kinase family of enzymes. The protein is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a c 0.1 mg
AR09001PU-N Adenylate kinase 3 (AK3) (aa 1_ 223) 0.5 mg
AK7 AK4 Gene adenylate kinase 4
AK5 AK3 Gene adenylate kinase 3
AK4 AK2 Gene adenylate kinase 2
AK3 AK1 Gene adenylate kinase 1
ARP41433_T100 Adenylate kinase 4 (AK4) 0.1 mg
GTX106079 Adenylate kinase 1 (AK1) 100 µl
AR09002PU-S Adenylate kinase 2 (AK2) (aa 1_ 239) 0.1 mg
GTX103629 Adenylate kinase 5 (AK5) 100 µl
ARP46059_T100 Adenylate kinase 2 (AK2) 0.1 mg
AR09001PU-S Adenylate kinase 3 (AK3) (aa 1_ 223) 0.1 mg
AR09002PU-N Adenylate kinase 2 (AK2) (aa 1_ 239) 0.5 mg
AR09002PU-S Adenylate kinase 2 (AK2) (aa 1_ 239) 0.1 mg
GTX111770 Adenylate kinase 7 (AK7) 100 µl
ARP48148_P050 Adenylate kinase 1 (AK1) 50 µg
AR09001PU-S Adenylate kinase 3 (AK3) (aa 1_ 223) 0.1 mg
AR09002PU-N Adenylate kinase 2 (AK2) (aa 1_ 239) 0.5 mg
ARP46059_T100 Adenylate kinase 2 (AK2) 100 µg
ARP41433_T100 Adenylate kinase 4 (AK4) 100 µg
SM6029S Adenylate kinase 3 (AK3) 50 µl
GTX107613 Adenylate kinase 2 (AK2) 100 µl
GTX107482 Adenylate kinase 3 (AK3) 100 µl
27840002 Adenylate kinase 1 (AK1) 100 µg


 

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