GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
4'-phosphopantetheinyl transferase Sfp (EC 2.7.8.7) (Surfactin synthase-activating enzyme)
SFP_BACSU Reviewed; 224 AA.
P39135;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
28-FEB-2018, entry version 119.
RecName: Full=4'-phosphopantetheinyl transferase Sfp;
EC=2.7.8.7 {ECO:0000269|PubMed:11451672};
AltName: Full=Surfactin synthase-activating enzyme;
Name=sfp; Synonyms=lpa-8; OrderedLocusNames=BSU03570;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
STRAIN=168, and oKB105;
PubMed=1557038;
Nakano M.M., Corbell N., Besson J., Zuber P.;
"Isolation and characterization of sfp: a gene that functions in the
production of the lipopeptide biosurfactant, surfactin, in Bacillus
subtilis.";
Mol. Gen. Genet. 232:313-321(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8407792; DOI=10.1128/jb.175.19.6203-6211.1993;
Grossman T.H., Tuckman M., Ellestad S., Osburne M.S.;
"Isolation and characterization of Bacillus subtilis genes involved in
siderophore biosynthesis: relationship between B. subtilis sfpo and
Escherichia coli entD genes.";
J. Bacteriol. 175:6203-6211(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH624, and ATCC 21332 / IAM 1213;
PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M.,
Venema G., van Sinderen D.;
"Sequence and analysis of the genetic locus responsible for surfactin
synthesis in Bacillus subtilis.";
Mol. Microbiol. 8:821-831(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=YB8;
PubMed=8639027; DOI=10.1007/s002030050322;
Tsuge K., Ano T., Shoda M.;
"Isolation of a gene essential for biosynthesis of the lipopeptide
antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8.";
Arch. Microbiol. 165:243-251(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[6]
SEQUENCE REVISION.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[7]
FUNCTION.
PubMed=8939709; DOI=10.1016/S1074-5521(96)90181-7;
Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
"A new enzyme superfamily -- the phosphopantetheinyl transferases.";
Chem. Biol. 3:923-936(1996).
[8]
CHARACTERIZATION, AND MUTAGENESIS OF GLY-105; ASP-107; TRP-147;
GLU-151 AND LYS-155.
PubMed=9484229; DOI=10.1021/bi9719861;
Quadri L.E.N., Weinreb P.H., Lei M., Nakano M.M., Zuber P.,
Walsh C.T.;
"Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl
transferase for peptidyl carrier protein domains in peptide
synthetases.";
Biochemistry 37:1585-1595(1998).
[9]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11451672; DOI=10.1016/S1074-5521(01)00047-3;
Sanchez C., Du L., Edwards D.J., Toney M.D., Shen B.;
"Cloning and characterization of a phosphopantetheinyl transferase
from Streptomyces verticillus ATCC15003, the producer of the hybrid
peptide-polyketide antitumor drug bleomycin.";
Chem. Biol. 8:725-738(2001).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=10581256; DOI=10.1093/emboj/18.23.6823;
Reuter K., Mofid M.R., Marahiel M.A., Ficner R.;
"Crystal structure of the surfactin synthetase-activating enzyme sfp:
a prototype of the 4'-phosphopantetheinyl transferase superfamily.";
EMBO J. 18:6823-6831(1999).
-!- FUNCTION: Activates the seven peptidyl carrier protein (PCP)
domains of surfactin synthase SRF1/2/3 by transferring the 4'-
phosphopantetheinyl moiety of coenzyme A (CoA) to a serine
residue. Required for cells of B.subtilis to become producers of
the lipopeptide antibiotics surfactin and plipastatin B1.
{ECO:0000269|PubMed:8939709}.
-!- CATALYTIC ACTIVITY: CoA-(4'-phosphopantetheine) + apo-[acyl-
carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-
carrier-protein]. {ECO:0000269|PubMed:11451672}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.7 uM for Streptomyces mobaraensis apo-PCP BlmI
{ECO:0000269|PubMed:9484229};
KM=11 uM for Streptomyces glaucescens apo-ACP TcmM
{ECO:0000269|PubMed:9484229};
Note=kcat is 7.2 min(-1) with S.mobaraensis apo-PCP BlmI as
substrate and 0.89 min(-1) with S.glaucescens apo-ACP TcmM as
substrate. {ECO:0000269|PubMed:9484229};
-!- SUBUNIT: Monomer in solution.
-!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
-!- CAUTION: Strain 168 and its derivatives encode a truncated,
inactive version of this protein. The sequence shown here
corresponds to that of strain ATCC 21332 which is active.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X63158; CAA44858.1; -; Genomic_DNA.
EMBL; X65610; CAA46561.1; -; Genomic_DNA.
EMBL; L17438; AAC36829.1; -; Unassigned_DNA.
EMBL; X70356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D50562; BAA09125.1; -; Genomic_DNA.
EMBL; AL009126; CAB12151.2; -; Genomic_DNA.
PIR; S20463; S20463.
PDB; 1QR0; X-ray; 1.90 A; A=1-224.
PDB; 2GE0; Model; -; A=1-224.
PDB; 2GE1; Model; -; A=1-224.
PDB; 4MRT; X-ray; 2.00 A; A=1-224.
PDBsum; 1QR0; -.
PDBsum; 2GE0; -.
PDBsum; 2GE1; -.
PDBsum; 4MRT; -.
ProteinModelPortal; P39135; -.
SMR; P39135; -.
STRING; 224308.Bsubs1_010100002028; -.
DrugBank; DB01992; Coenzyme A.
PaxDb; P39135; -.
eggNOG; ENOG4105W8Z; Bacteria.
eggNOG; COG2091; LUCA.
InParanoid; P39135; -.
BioCyc; MetaCyc:MONOMER-13919; -.
EvolutionaryTrace; P39135; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
GO; GO:1900192; P:positive regulation of single-species biofilm formation; IMP:CACAO.
Gene3D; 3.90.470.20; -; 3.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
Pfam; PF01648; ACPS; 1.
SUPFAM; SSF56214; SSF56214; 2.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Complete proteome;
Direct protein sequencing; Magnesium; Metal-binding;
Reference proteome; Transferase.
CHAIN 1 224 4'-phosphopantetheinyl transferase Sfp.
/FTId=PRO_0000206077.
REGION 158 189 Peptidyl carrier protein binding.
{ECO:0000255}.
METAL 107 107 Magnesium.
METAL 109 109 Magnesium.
METAL 151 151 Magnesium.
VARIANT 22 22 S -> T (in strain: oKB105).
VARIANT 97 97 C -> G (in strain: oKB105).
VARIANT 157 224 EGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVD
PGYKMAVCAAHPDFPEDITMVSYEELL -> GRQRLIASA
(in strain 168 and its derivatives, non
surfactin-producing strains).
MUTAGEN 105 105 G->A: Almost no activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 105 105 G->D: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 107 107 D->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 107 107 D->E: 3000-fold reduction in activity,
but no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 147 147 W->A: 24-fold reduction in activity, but
no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 147 147 W->F: 5-fold reduction in activity, but
no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 151 151 E->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 155 155 K->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
CONFLICT 118 119 IA -> MP (in Ref. 3; CAA46561).
{ECO:0000305}.
STRAND 2 7 {ECO:0000244|PDB:1QR0}.
HELIX 14 21 {ECO:0000244|PDB:1QR0}.
HELIX 26 34 {ECO:0000244|PDB:1QR0}.
HELIX 38 58 {ECO:0000244|PDB:1QR0}.
HELIX 63 65 {ECO:0000244|PDB:1QR0}.
STRAND 85 91 {ECO:0000244|PDB:1QR0}.
STRAND 94 102 {ECO:0000244|PDB:1QR0}.
STRAND 105 110 {ECO:0000244|PDB:1QR0}.
HELIX 116 119 {ECO:0000244|PDB:1QR0}.
STRAND 120 123 {ECO:0000244|PDB:1QR0}.
HELIX 125 133 {ECO:0000244|PDB:1QR0}.
HELIX 136 157 {ECO:0000244|PDB:1QR0}.
HELIX 160 162 {ECO:0000244|PDB:4MRT}.
HELIX 165 167 {ECO:0000244|PDB:4MRT}.
STRAND 169 172 {ECO:0000244|PDB:1QR0}.
HELIX 174 176 {ECO:0000244|PDB:1QR0}.
STRAND 178 181 {ECO:0000244|PDB:1QR0}.
STRAND 190 194 {ECO:0000244|PDB:1QR0}.
STRAND 200 209 {ECO:0000244|PDB:1QR0}.
HELIX 220 224 {ECO:0000244|PDB:1QR0}.
SEQUENCE 224 AA; 26168 MW; 0FEFB5D9D3534C68 CRC64;
MKIYGIYMDR PLSQEENERF MSFISPEKRE KCRRFYHKED AHRTLLGDVL VRSVISRQYQ
LDKSDIRFST QEYGKPCIPD LPDAHFNISH SGRWVICAFD SQPIGIDIEK TKPISLEIAK
RFFSKTEYSD LLAKDKDEQT DYFYHLWSMK ESFIKQEGKG LSLPLDSFSV RLHQDGQVSI
ELPDSHSPCY IKTYEVDPGY KMAVCAAHPD FPEDITMVSY EELL
Related products :
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
Pathways :
No related Items
Related Genes :
[AASDHPPT CGI-80 HAH-P HSPC223 x0005] L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC 2.7.8.-) (4'-phosphopantetheinyl transferase) (Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase) (AASD-PPT) (LYS5 ortholog)
[sfp lpa-8 BSU03570] 4'-phosphopantetheinyl transferase Sfp (EC 2.7.8.7) (Surfactin synthase-activating enzyme)
[acpS dpj b2563 JW2547] Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
[nnr acpS nnrD CLPU_4c02320] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD TR13x_08920] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[nnr_1 acpS nnrD PP176A_2022] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD DW1_2354] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[entD b0583 JW5085] Enterobactin synthase component D (4'-phosphopantetheinyl transferase EntD) (EC 2.7.8.-) (Enterochelin synthase D)
[nnrD acpS L21TH_2442] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD Y919_05665] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD SAMN02745135_01025] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD SAMN02745784_01406] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[nnrD acpS SAMN05660462_03058] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD SAMN05660923_01008] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[npgA cfwA ANIA_06140] 4'-phosphopantetheinyl transferase NpgA (PPTase) (EC 2.7.8.7)
[nnrD acpS AUH82_02110] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS WT2_00416] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); Alanine racemase (EC 5.1.1.1)]
[acpS nagZ Aave_1200] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); Beta-hexosaminidase (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (N-acetyl-beta-glucosaminidase)]
[lpa-14 lpaA13 lpaB3 sfp-B] 4'-phosphopantetheinyl transferase (EC 2.7.8.-) (Lipopeptide antibiotics iturin A and surfactin biosynthesis protein)
[lys7 SPAC17C9.02c] L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASD-PPT) (EC 2.7.8.7)
[orsA AN7909] Orsellinic acid synthase (OAS) (EC 2.3.1.-) (Non-reducing polyketide synthase orsA) (Orsellinic acid/F9775 biosynthesis cluster protein A)
[mdpG AN0150] Atrochrysone carboxylic acid synthase (ACAS) (EC 2.3.1.-) (Monodictyphenone synthesis protein G) (Non-reducing polyketide synthase mdpG)
[Aasdhppt] L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC 2.7.8.-) (4'-phosphopantetheinyl transferase) (Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase) (AASD-PPT)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like proteinase (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.69) (Non-structural protein 3) (nsp3); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Guanine-N7 methyltransferase (ExoN) (EC 2.1.1.-) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (nsp16)]
[acpS nnrD HMPREF1864_00276] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD HMPREF9625_00660] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD Curi_c20840] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[nnrD acpS ING2D1G_0327] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[nnrD acpS CLCY_1c03490] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
[acpS nnrD XD91_0345] Multifunctional fusion protein [Includes: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS); ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase)]
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits