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Protein
Submitted name:

Fengycin synthetase

Gene

fenB

Organism
Bacillus subtilis
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Protein family/group databases

ESTHERibacsu-FENB. Thioesterase.

Names & Taxonomyi

Protein namesi
Submitted name:
Fengycin synthetaseImported
Gene namesi
Name:fenBImported
OrganismiBacillus subtilisImported
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CB9X-ray1.80A1043-1274[»]
2CBGX-ray2.50A1043-1274[»]
ProteinModelPortaliQ45563.
SMRiQ45563. Positions 1045-1263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45563.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini973 – 104068Acyl carrierInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.SAAS annotation

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020459. AMP-binding.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
PRINTSiPR00154. AMPBINDING.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q45563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKTKKIKNV YPLSHMQEGM LFHSFLHKEE GAYVEQSLFT IKGSLSYEIF
60 70 80 90 100
QRSIQAIIDR HDIFRTVFLP HVPNLSGPRQ VVMTERNFHL HTEDISSLQT
110 120 130 140 150
NEQNDYIEQF KEKDKKKGFD LQKDMLMRIS LLKTAENEHV CVWSHHHILM
160 170 180 190 200
DGWCLGIILQ EFMQIYQSIH TGNHLALEPV RPYSTYISWL TKQDKETAAD
210 220 230 240 250
YWRAYLKNYS TPSQLPRVTD REAKEGYYRE ELIFTLNQKL TDKLKETAKQ
260 270 280 290 300
TGVTLATFIQ TVWGVMLQRY NRTDDVVFGA VVSGRPSEIP GVESMIGLFI
310 320 330 340 350
NTVPVRVKTG KEETFAELLS RCQQDMLDAE PFTCHPLFDI QANTALKQEL
360 370 380 390 400
IDHIIVFENY PLQQKMADSA DQIDSPLQID NVKVSEQSGY NFNLVVAPGD
410 420 430 440 450
ELVIKFSYNA HVYDAAWMTC IQRQLTQALQ AAADHPDIPV ADFSFLDPKE
460 470 480 490 500
KEQILTQCND TSTAYPKNKT VIDIFREQTV KTPDQTALVY GNRSISYREL
510 520 530 540 550
DQKSDALART LYENGLRRNG TAGILAGHSP EFIISVLAVL KAGGTYLPLD
560 570 580 590 600
AELPPERISY MLSETKAAIL IVQKGLEPNT AFAGTFISAD AEAMIEEHTK
610 620 630 640 650
PLEIVTGPDD LAYIMYTSGS TGRPKGVMIT NRNVVSLVCN SNYTSASVND
660 670 680 690 700
RFILTGSISF DAVTFEMFGA LLKGATLHII DKSTMLTPDR FGAYLIENNI
710 720 730 740 750
TVLFLTTALF NQLAQAQADM FHRLHTLYVG GEALSPELIN AVRRACPNLS
760 770 780 790 800
LYNIYGPTEN TTFSTFFEIK RDYATPIPIG KPISNCTAFI LDAKGCLLPI
810 820 830 840 850
GVPGELCVGG DGVAKGYLNR DDVTAAVFSP DPFIPGERIY RTGDLARWLP
860 870 880 890 900
DGNLEYISRI DRQIKIRGKR IEPAEIEARL LEIEGVREAA VTLLETDGEV
910 920 930 940 950
QLYTHYVSDE SRNEKEIRAA LARVLPDYMI PQRWVRVDRM PLTGNGKINR
960 970 980 990 1000
SALPVPENES ENRQDLTPPR NWVEQELTQI WKSVLGVKTI GIHDDFFALG
1010 1020 1030 1040 1050
GHSLKALQVI HMLKHHQHVD IPIDVLFENP TIAQLAEKLY SNQLSAAGEQ
1060 1070 1080 1090 1100
HVIQLNQQGG KNLFCFPPIS GFGIYFKDLA LQLNHKAAVY GFHFIEEDSR
1110 1120 1130 1140 1150
IEQYVSRITE IQPEGPYVLL GYSAGGNLAF EVVQAMEQKG LEVSDFIIVD
1160 1170 1180 1190 1200
AYKKDQSITA DTENDDSAAY LPEAVRETVM QKKRCYQEYW AQLINEGRIK
1210 1220 1230 1240 1250
SNIHFIEAGI QTETSGAMVL QKWQDAAEEG YAEYTGYGAH KDMLEGEFAE
1260 1270
KNANIILNIL DKINSDQKVL PNKH
Length:1,274
Mass (Da):143,630
Last modified:November 1, 1996 - v1
Checksum:i068DA342F321CE95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42523 Genomic DNA. Translation: AAB00093.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42523 Genomic DNA. Translation: AAB00093.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CB9X-ray1.80A1043-1274[»]
2CBGX-ray2.50A1043-1274[»]
ProteinModelPortaliQ45563.
SMRiQ45563. Positions 1045-1263.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibacsu-FENB. Thioesterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ45563.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020459. AMP-binding.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
PRINTSiPR00154. AMPBINDING.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ45563_BACIU
AccessioniPrimary (citable) accession number: Q45563
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.