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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)DescriptionActionsGraphical viewLength
Binding sitei228Pyridoxal phosphate; via amide nitrogenBy similarity1
Binding sitei272SubstrateBy similarity1
Binding sitei375Pyridoxal phosphateBy similarity1
Binding sitei375SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004217561 – 428L-glutamyl-[BtrI acyl-carrier protein] decarboxylaseAdd BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Beta strandi17 – 23Combined sources7
Helixi24 – 36Combined sources13
Beta strandi42 – 47Combined sources6
Helixi48 – 50Combined sources3
Helixi54 – 62Combined sources9
Beta strandi66 – 71Combined sources6
Helixi72 – 80Combined sources9
Helixi85 – 87Combined sources3
Beta strandi88 – 90Combined sources3
Helixi97 – 106Combined sources10
Beta strandi109 – 113Combined sources5
Helixi116 – 129Combined sources14
Beta strandi133 – 140Combined sources8
Beta strandi151 – 153Combined sources3
Beta strandi158 – 162Combined sources5
Helixi163 – 165Combined sources3
Helixi166 – 175Combined sources10
Beta strandi179 – 185Combined sources7
Helixi195 – 216Combined sources22
Beta strandi221 – 224Combined sources4
Helixi242 – 257Combined sources16
Turni258 – 260Combined sources3
Beta strandi265 – 271Combined sources7
Helixi272 – 275Combined sources4
Helixi276 – 278Combined sources3
Beta strandi279 – 291Combined sources13
Beta strandi294 – 300Combined sources7
Turni303 – 305Combined sources3
Beta strandi322 – 325Combined sources4
Beta strandi337 – 342Combined sources6
Beta strandi344 – 347Combined sources4
Beta strandi351 – 359Combined sources9
Beta strandi366 – 371Combined sources6
Beta strandi373 – 376Combined sources4
Helixi377 – 379Combined sources3
Helixi384 – 386Combined sources3
Beta strandi391 – 396Combined sources6
Beta strandi399 – 404Combined sources6
Helixi409 – 413Combined sources5
Helixi414 – 416Combined sources3

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 272Pyridoxal phosphate bindingBy similarity4

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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J66X-ray1.65A1-428[»]
ProteinModelPortaliQ2L4H3.
SMRiQ2L4H3.
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...

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: November 2, 2016
This is version 49 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.