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Protein

L-glutamyl-[BtrI acyl-carrier protein] decarboxylase

Gene

btrK

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyridoxal phosphate-dependent decarboxylase that catalyzes 1 step in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Able to decarboxylate L-ornithine, L-arginine, L-lysine, but not L-glutamate or any D-amino acids. Has low activity with substrates not bound to an acyl-carrier protein.1 Publication

Catalytic activityi

L-glutamyl-[BtrI acyl-carrier protein] = 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Pathwayi: butirosin biosynthesis

This protein is involved in the pathway butirosin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway butirosin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei228 – 2281Pyridoxal phosphate; via amide nitrogenBy similarity
Binding sitei272 – 2721SubstrateBy similarity
Binding sitei375 – 3751Pyridoxal phosphateBy similarity
Binding sitei375 – 3751SubstrateBy similarity

GO - Molecular functioni

  • carboxy-lyase activity Source: UniProtKB
  • diaminopimelate decarboxylase activity Source: InterPro
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00964.

Names & Taxonomyi

Protein namesi
Recommended name:
L-glutamyl-[BtrI acyl-carrier protein] decarboxylase (EC:4.1.1.95)
Alternative name(s):
Butirosin biosynthesis protein K
Gene namesi
Name:btrK
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428L-glutamyl-[BtrI acyl-carrier protein] decarboxylasePRO_0000421756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Beta strandi17 – 237Combined sources
Helixi24 – 3613Combined sources
Beta strandi42 – 476Combined sources
Helixi48 – 503Combined sources
Helixi54 – 629Combined sources
Beta strandi66 – 716Combined sources
Helixi72 – 809Combined sources
Helixi85 – 873Combined sources
Beta strandi88 – 903Combined sources
Helixi97 – 10610Combined sources
Beta strandi109 – 1135Combined sources
Helixi116 – 12914Combined sources
Beta strandi133 – 1408Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi158 – 1625Combined sources
Helixi163 – 1653Combined sources
Helixi166 – 17510Combined sources
Beta strandi179 – 1857Combined sources
Helixi195 – 21622Combined sources
Beta strandi221 – 2244Combined sources
Helixi242 – 25716Combined sources
Turni258 – 2603Combined sources
Beta strandi265 – 2717Combined sources
Helixi272 – 2754Combined sources
Helixi276 – 2783Combined sources
Beta strandi279 – 29113Combined sources
Beta strandi294 – 3007Combined sources
Turni303 – 3053Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi337 – 3426Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi351 – 3599Combined sources
Beta strandi366 – 3716Combined sources
Beta strandi373 – 3764Combined sources
Helixi377 – 3793Combined sources
Helixi384 – 3863Combined sources
Beta strandi391 – 3966Combined sources
Beta strandi399 – 4046Combined sources
Helixi409 – 4135Combined sources
Helixi414 – 4163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J66X-ray1.65A1-428[»]
ProteinModelPortaliQ2L4H3.
SMRiQ2L4H3. Positions 4-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2724Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

KOiK13560.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2L4H3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLDQAEITA LTKRFETPFY LYDGDFIEAH YRQLRSRTNP AIQFYLSLKA
60 70 80 90 100
NNNIHLAKLF RQWGLGVEVA SAGELALARH AGFSAENIIF SGPGKKRSEL
110 120 130 140 150
EIAVQSGIYC IIAESVEELF YIEELAEKEN KTARVAIRIN PDKSFGSTAI
160 170 180 190 200
KMGGVPRQFG MDESMLDAVM DAVRSLQFTK FIGIHVYTGT QNLNTDSIIE
210 220 230 240 250
SMKYTVDLGR NIYERYGIVC ECINLGGGFG VPYFSHEKAL DIGKITRTVS
260 270 280 290 300
DYVQEARDTR FPQTTFIIES GRYLLAQAAV YVTEVLYRKA SKGEVFVIVD
310 320 330 340 350
GGMHHHAAST FRGRSMRSNY PMEYIPVRED SGRRELEKVT IAGPLCTPED
360 370 380 390 400
CLGKDVHVPA LYPGDLVCVL NSGAYGLSFS PVHFLGHPTP IEILKRNGSY
410 420
ELIRRKGTAD DIVATQLQTE SNLLFVDK
Length:428
Mass (Da):47,816
Last modified:March 6, 2013 - v2
Checksum:i4545F7F69D0AFEC7
GO

Sequence cautioni

The sequence CAG77429.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB097196 Genomic DNA. Translation: BAE07075.1.
AJ781030 Genomic DNA. Translation: CAG77429.1. Different initiation.

Genome annotation databases

KEGGiag:BAE07075.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB097196 Genomic DNA. Translation: BAE07075.1.
AJ781030 Genomic DNA. Translation: CAG77429.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J66X-ray1.65A1-428[»]
ProteinModelPortaliQ2L4H3.
SMRiQ2L4H3. Positions 4-417.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAE07075.

Phylogenomic databases

KOiK13560.

Enzyme and pathway databases

UniPathwayiUPA00964.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Extended sequence and functional analysis of the butirosin biosynthetic gene cluster in Bacillus circulans SANK 72073."
    Kudo F., Numakura M., Tamegai H., Yamamoto H., Eguchi T., Kakinuma K.
    J. Antibiot. 58:373-379(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21557 / NCIB 12336.
  2. "Analysis and comparison of the biosynthetic gene clusters for the 2-deoxystreptamine-containing aminoglycoside antibiotics ribostamycin, neomycin, lividomycin, paromomycin and butirosin."
    Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A., Piepersberg W.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21557 / NCIB 12336.
  3. "Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway."
    Li Y., Llewellyn N.M., Giri R., Huang F., Spencer J.B.
    Chem. Biol. 12:665-675(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT.
    Strain: ATCC 21557 / NCIB 12336.
  4. "Structural characterisation of Btrk decarboxylase from Bacillus circulans butirosin biosynthesis."
    Popovic B., Li Y., Chirgadze D.Y., Blundell T.L., Spencer J.B.
    Submitted (SEP-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR.

Entry informationi

Entry nameiBTRK_BACCI
AccessioniPrimary (citable) accession number: Q2L4H3
Secondary accession number(s): Q4H4E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 6, 2013
Last modified: January 20, 2016
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.