O57883 (O57883_PYRHO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
235aa long hypothetical biotin--[acetyl-CoA-carboxylase] ligase EMBL BAA29216.1

Gene names

Ordered Locus Names:

PH0147

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	ATP-binding PDB 2DTO PDB 2DXT PDB 1X01 Biotin PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW PDB 2EJF Nucleotide-binding
Molecular function	Ligase EMBL BAA29216.1
Technical term	3D-structure PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW PDB 1WNL PDB 1X01 PDB 2EJF PDB 2DEQ PDB 2DJZ PDB 2DZC PDB 2EJG PDB 2DXU PDB 2E41 PDB 2E64 PDB 2E65 PDB 2E10 PDB 2DVE PDB 2DKG PDB 2HNI PDB 1WQW PDB 1WQ7 PDB 2E1H PDB 2DTI PDB 2DZ9 Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	48 – 54	7	ADP PDB 2DTH PDB 2FYK PDB 1WNL
	Nucleotide binding	48 – 54	7	ATP PDB 2DTO PDB 2DXT PDB 1X01
	Nucleotide binding	100 – 104	5	ATP PDB 2DTO PDB 2DXT PDB 1X01
	Nucleotide binding	103 – 104	2	ADP PDB 2FYK
	Nucleotide binding	231 – 233	3	ATP PDB 2DTO
	Region	21 – 23	3	Biotin 1 binding PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW
	Region	46 – 53	8	Biotin 1 binding PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW
	Region	103 – 104	2	Biotin 1 binding PDB 1WPY PDB 2DTO PDB 2FYK PDB 2ZGW
Sites
	Binding site	42	1	Biotin 1 PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW
	Binding site	111	1	ADP PDB 2FYK PDB 1WNL
	Binding site	111	1	ATP PDB 2DTO PDB 2DXT PDB 1X01
	Binding site	111	1	Biotin 1 PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK
	Binding site	115	1	Biotin 1 PDB 1WPY PDB 2DTH PDB 2DTO PDB 2DXT PDB 2FYK PDB 2ZGW
	Binding site	131	1	ADP PDB 2DTH PDB 2FYK PDB 1WNL
	Binding site	131	1	ATP PDB 2DTO PDB 2DXT PDB 1X01
	Binding site	211	1	Biotin 2 PDB 2EJF
	Binding site	227	1	ATP PDB 2DTO PDB 2DXT
	Binding site	227	1	Biotin 2; via amide nitrogen PDB 2EJF
	Binding site	233	1	ADP PDB 1WNL

Sequences

	Sequence		Length	Mass (Da)
	O57883 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 65C77DFB16A3F029	FASTA	235	26,072
	10 20 30 40 50 60 MLGLKTSIIG RRVIYFQEIT STNEFAKTSY LEEGTVIVAD KQTMGHGRLN RKWESPEGGL 70 80 90 100 110 120 WLSIVLSPKV PQKDLPKIVF LGAVGVVETL KEFSIDGRIK WPNDVLVNYK KIAGVLVEGK 130 140 150 160 170 180 GDKIVLGIGL NVNNKVPNGA TSMKLELGSE VPLLSVFRSL ITNLDRLYLN FLKNPMDILN 190 200 210 220 230 LVRDNMILGV RVKILGDGSF EGIAEDIDDF GRLIIRLDSG EVKKVIYGDV SLRFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 and OT3.
[2]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3." Bagautdinov B., Kunishima N. Submitted (FEB-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[3]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3." Bagautdinov B., Kunishima N. Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[4]	"Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate." Bagautdinov B., Matsuura Y., Bagautdinova S., Kunishima N. J. Biol. Chem. 283:14739-14750(2008) [PubMed: 18372281] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH ATP AND BIOTIN.
[5]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (DEC-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[6]	"Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (OCT-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[7]	"Ligand Structures of Biotin Protein Ligase From Pyrococcus Horikoshii OT3." Bagautdinov B., Kunishima N. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
[8]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[9]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ADP AND BIOTIN.
[10]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3." Bagautdinov B., Kunishima N. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
[11]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Matsuura Y., Kunishima N. Submitted (AUG-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP AND BIOTIN.
[12]	"Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation." Bagautdinov B., Kuroishi C., Sugahara M., Kunishima N. J. Mol. Biol. 353:322-333(2005) [PubMed: 16169557] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ADP AND BIOTIN.
[13]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (OCT-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).
[14]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Kunishima N. Submitted (FEB-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ADP AND BIOTIN.
[15]	"Ligand Structures Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3." Bagautdinov B., Matsuura Y., Kunishima N. Submitted (SEP-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA29216.1.

PIR

A71236.

RefSeq

NP_142152.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WNL	X-ray	1.60	A/B	1-235	[»]
1WPY	X-ray	1.60	A/B	1-235	[»]
1WQ7	X-ray	1.60	A/B	1-235	[»]
1WQW	X-ray	1.45	A/B	1-235	[»]
1X01	X-ray	2.00	A/B	1-235	[»]
2DEQ	X-ray	1.85	A/B	1-235	[»]
2DJZ	X-ray	1.85	A/B	1-235	[»]
2DKG	X-ray	2.00	A/B	1-235	[»]
2DTH	X-ray	1.95	A/B	1-235	[»]
2DTI	X-ray	2.20	A/B	1-235	[»]
2DTO	X-ray	1.50	A/B	1-235	[»]
2DVE	X-ray	1.60	A/B	1-235	[»]
2DXT	X-ray	1.60	A/B	1-235	[»]
2DXU	X-ray	1.28	A/B	1-235	[»]
2DZ9	X-ray	1.84	A/B	1-235	[»]
2DZC	X-ray	1.45	A/B	1-235	[»]
2E10	X-ray	1.35	A/B	1-235	[»]
2E1H	X-ray	1.40	A/B	1-235	[»]
2E41	X-ray	1.75	A/B	1-235	[»]
2E64	X-ray	1.50	A/B	1-235	[»]
2E65	X-ray	1.65	A/B	1-235	[»]
2EJF	X-ray	2.00	A/B	1-235	[»]
2EJG	X-ray	2.71	A/B	1-235	[»]
2FYK	X-ray	1.60	A/B	1-235	[»]
2HNI	X-ray	1.90	A/B	1-235	[»]
2ZGW	X-ray	1.50	A/B	1-235	[»]

ProteinModelPortal

O57883.

SMR

O57883. Positions 1-235.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001632; EBPYRP00000001632; EBPYRG00000001632.

GeneID

1444041.

GenomeReviews

Gene locus PH0147 in contig BA000001_GR.

KEGG

pho:PH0147.

NMPDR

fig|70601.1.peg.141.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022717.

HOGENOM

HBG750923.

OMA

QTMGHGR.

ProtClustDB

PRK08330.

Enzyme and pathway databases

BioCyc

PHOR70601:PH0147-MONOMER.

Family and domain databases

InterPro

IPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR008988. Transcriptional_repressor_C.
[Graphical view]

KO

K03524.

PANTHER

PTHR12835. BirA_ligase. 1 hit.

Pfam

PF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]

SUPFAM

SSF50037. Transcr_rep_C. 1 hit.

TIGRFAMs

TIGR00121. BirA_ligase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

O57883_PYRHO

Accession

Primary (citable) accession number: O57883

Entry history

Integrated into UniProtKB/TrEMBL:	August 1, 1998
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)