Reviewed, UniProtKB/Swiss-Prot O14353 (BPL1_SCHPO)

Names and origin

Protein names

Recommended name:
    Biotin--protein ligase
    EC=6.3.4.-
Alternative name(s):
    Biotin apo-protein ligase
Including the following 4 domains:
    1- Recommended name:
            Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
              EC=6.3.4.9
    2- Recommended name:
            Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
              EC=6.3.4.10
        Alternative name(s):
            Holocarboxylase synthetase
              Short name=HCS
    3- Recommended name:
            Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
              EC=6.3.4.11
    4- Recommended name:
            Biotin--[acetyl-CoA-carboxylase] ligase
              EC=6.3.4.15

Gene names

Name:	bpl1
ORF Names:	SPBC30D10.07c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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.
Catalytic activity	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)].
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the biotin--protein ligase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity Inferred from electronic annotation. Source: EC biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 631	631	Biotin--protein ligase		PRO_0000315970

Sequences

	Sequence		Length	Mass (Da)
	O14353-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 37E08571359F5112	FASTA	631	70,632
	10 20 30 40 50 60 MNVLIYNGNG ASKICLLRTF QSLLPFVVPL YAMRFVDAST LEKEPWPAST ALLVMPGGRD 70 80 90 100 110 120 MGYCSSFNET IYRKITDFVK RGGAYLGLCA GGYFGSAVVD FRMPDSDLNV VGKRKLQFFP 130 140 150 160 170 180 GTCAGPTFPG FTYDSEDGAR RASIIVDGMQ SSPVHTHIYF NGGGSFLETE NYSNVKVVAR 190 200 210 220 230 240 YQETDFEKSA AIIYVKVGKG NVVLTGIHPE FSAEGSPILD KRDEKTRLEL LSYILKLLGL 250 260 270 280 290 300 KVPKDTSKCG QPTLTDQYLF PNNVETKRFI EKALTNKVKN QDEDTLYTFQ FSDISSEIPE 310 320 330 340 350 360 HQLANLDISA DLSDSDNEIV KIWYGDEEKI CKKAKPSFDL ELYAKLINGC RFGLPIIVAP 370 380 390 400 410 420 VIRSTQTLLD KNYRFLDSTN TGFTVLGNYQ TAGRGRGQNM WVSPYGTLAF SFIINVDAKN 430 440 450 460 470 480 FSTTPIALFQ YLMALAVVRG IREYAPGYEN IPAFIKWPND VYVRVDKGGI NFQGKQYMKL 490 500 510 520 530 540 SGIIVTSNYR KNVLHLVVGC GINVSNLGPT VSLNTLVDEW NKNSDNPRLE KFSFEKLLAS 550 560 570 580 590 600 VLNQFDRYHR LLLEEGFSLI LPEYYQYWLH SNQTVNLASG GKAIIQGITS DFGFLLAQLL 610 620 630 NENNEPTTKV VHLQPDGNSF DLMRNLITRK T

References

[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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAB10802.1.
PIR	T40189.
RefSeq	NP_596278.1.
3D structure databases
SMR	O14353. Positions 355-597.
ModBase	Search...
Protein-protein interaction databases
STRING	O14353.
Genome annotation databases
GeneID	2540476.
GenomeReviews	Gene locus bpl1 in contig CU329671_GR.
KEGG	spo:SPBC30D10.07c.
NMPDR	fig|4896.1.peg.2144.
Organism-specific databases
GeneDB_Spombe	SPBC30D10.07c.
Phylogenomic databases
eggNOG	fuNOG04506.
HOGENOM	HBG734872.
OMA	CAGGYYG.
OrthoDB	EOG9BRZ33.
PhylomeDB	O14353.
Enzyme and pathway databases
BRENDA	6.3.4.10. 653. 6.3.4.11. 653. 6.3.4.15. 653. 6.3.4.9. 653.
Gene expression databases
ArrayExpress	O14353.
Family and domain databases
InterPro	IPR004408. Biotin_CoA_COase_ligase. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. [Graphical view]
PANTHER	PTHR12835. BirA_ligase. 1 hit.
Pfam	PF02237. BPL_C. 1 hit. PF03099. BPL_LipA_LipB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00121. birA_ligase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BPL1_SCHPO

Accession

Primary (citable) accession number: O14353

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)