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Protein

Biotin--protein ligase

Gene

bpl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase (By similarity).By similarity

Catalytic activityi

ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase].
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)].
ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. biotin-[acetyl-CoA-carboxylase] ligase activity Source: UniProtKB-EC
  3. biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity Source: UniProtKB-EC
  4. biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity Source: UniProtKB-EC
  5. biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity Source: UniProtKB-EC
  6. biotin-protein ligase activity Source: PomBase

GO - Biological processi

  1. protein biotinylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188246. Biotin transport and metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin--protein ligase (EC:6.3.4.-)
Alternative name(s):
Biotin apo-protein ligase
Including the following 4 domains:
Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC:6.3.4.9)
Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC:6.3.4.10)
Alternative name(s):
Holocarboxylase synthetase
Short name:
HCS
Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC:6.3.4.11)
Biotin--[acetyl-CoA-carboxylase] ligase (EC:6.3.4.15)
Gene namesi
Name:bpl1
ORF Names:SPBC30D10.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC30D10.07c.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631Biotin--protein ligasePRO_0000315970Add
BLAST

Proteomic databases

MaxQBiO14353.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi4896.SPBC30D10.07c-1.

Structurei

3D structure databases

ProteinModelPortaliO14353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 553213BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the biotin--protein ligase family.Curated
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0340.
HOGENOMiHOG000214585.
InParanoidiO14353.
KOiK01942.
OMAiCEFEVGN.
OrthoDBiEOG7KQ2BG.
PhylomeDBiO14353.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR019197. Biotin-prot_ligase_N.
IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF09825. BPL_N. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14353-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVLIYNGNG ASKICLLRTF QSLLPFVVPL YAMRFVDAST LEKEPWPAST
60 70 80 90 100
ALLVMPGGRD MGYCSSFNET IYRKITDFVK RGGAYLGLCA GGYFGSAVVD
110 120 130 140 150
FRMPDSDLNV VGKRKLQFFP GTCAGPTFPG FTYDSEDGAR RASIIVDGMQ
160 170 180 190 200
SSPVHTHIYF NGGGSFLETE NYSNVKVVAR YQETDFEKSA AIIYVKVGKG
210 220 230 240 250
NVVLTGIHPE FSAEGSPILD KRDEKTRLEL LSYILKLLGL KVPKDTSKCG
260 270 280 290 300
QPTLTDQYLF PNNVETKRFI EKALTNKVKN QDEDTLYTFQ FSDISSEIPE
310 320 330 340 350
HQLANLDISA DLSDSDNEIV KIWYGDEEKI CKKAKPSFDL ELYAKLINGC
360 370 380 390 400
RFGLPIIVAP VIRSTQTLLD KNYRFLDSTN TGFTVLGNYQ TAGRGRGQNM
410 420 430 440 450
WVSPYGTLAF SFIINVDAKN FSTTPIALFQ YLMALAVVRG IREYAPGYEN
460 470 480 490 500
IPAFIKWPND VYVRVDKGGI NFQGKQYMKL SGIIVTSNYR KNVLHLVVGC
510 520 530 540 550
GINVSNLGPT VSLNTLVDEW NKNSDNPRLE KFSFEKLLAS VLNQFDRYHR
560 570 580 590 600
LLLEEGFSLI LPEYYQYWLH SNQTVNLASG GKAIIQGITS DFGFLLAQLL
610 620 630
NENNEPTTKV VHLQPDGNSF DLMRNLITRK T
Length:631
Mass (Da):70,632
Last modified:January 1, 1998 - v1
Checksum:i37E08571359F5112
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB10802.1.
PIRiT40189.
RefSeqiNP_596278.1. NM_001022199.2.

Genome annotation databases

EnsemblFungiiSPBC30D10.07c.1; SPBC30D10.07c.1:pep; SPBC30D10.07c.
GeneIDi2540476.
KEGGispo:SPBC30D10.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB10802.1.
PIRiT40189.
RefSeqiNP_596278.1. NM_001022199.2.

3D structure databases

ProteinModelPortaliO14353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4896.SPBC30D10.07c-1.

Proteomic databases

MaxQBiO14353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC30D10.07c.1; SPBC30D10.07c.1:pep; SPBC30D10.07c.
GeneIDi2540476.
KEGGispo:SPBC30D10.07c.

Organism-specific databases

PomBaseiSPBC30D10.07c.

Phylogenomic databases

eggNOGiCOG0340.
HOGENOMiHOG000214585.
InParanoidiO14353.
KOiK01942.
OMAiCEFEVGN.
OrthoDBiEOG7KQ2BG.
PhylomeDBiO14353.

Enzyme and pathway databases

ReactomeiREACT_188246. Biotin transport and metabolism.

Miscellaneous databases

NextBioi20801603.
PROiO14353.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR019197. Biotin-prot_ligase_N.
IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF09825. BPL_N. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiBPL1_SCHPO
AccessioniPrimary (citable) accession number: O14353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.