Q9X1M1 (Q9X1M1_THEMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Octoprenyl-diphosphate synthase, putative EMBL AAD36602.1

Gene names

Ordered Locus Names:

TM_1535

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the FPP/GGPP synthase family. RuleBase RU004466

Ontologies

Keywords
Biological process	Isoprene biosynthesis RuleBase RU004466
Molecular function	Transferase RuleBase RU004466
Technical term	3D-structure PDB 1WL1 PDB 1WKZ PDB 2AZL PDB 1V4E PDB 1VG3 PDB 1V4I PDB 1V4J PDB 1V4H PDB 1V4K PDB 1WL2 PDB 1WL3 PDB 1WL0 PDB 1VG4 PDB 1VG2 PDB 1VG7 PDB 1VG6 Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9X1M1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 8924C8CD98C418F9	FASTA	299	33,858
	10 20 30 40 50 60 MTKNKLNQNS YELEKVKERI EQILSQFFPE QIMKDLPLYG KMLRVRLSIL SFKNRGVEIG 70 80 90 100 110 120 EDAISSLAAL ELVHLASLLH DDVIDGARFR RGKETINFMY GDKAAVAAGD LVLVSAFHTV 130 140 150 160 170 180 EEIGNNKLRR AFLNVIGKMS EAELIEQLSR YKPITKEEYL RIVEGKSGAL FGLALQLPAL 190 200 210 220 230 240 LEGELGEDLY NLGVTIGTIY QMFDDIMDFA GMEKIGKDGF LDLKNGVASF PLVTAMEKFP 250 260 270 280 290 EARQMFENRD WSGLMSFMRE KGILKECEET LKVLVKNVII ENSWLRDFVD GIFKIKISS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination." Guo R.T., Kuo C.J., Chou C.C., Ko T.P., Shr H.L., Liang P.H., Wang A.H. J. Biol. Chem. 279:4903-4912(2004) [PubMed: 14617622] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS).
[3]	"A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products." Guo R.T., Kuo C.J., Ko T.P., Chou C.C., Liang P.H., Wang A.H. Biochemistry 43:7678-7686(2004) [PubMed: 15196010] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
[4]	"Biochemical and Structural Basis for Octaprenyl Pyrophosphate Synthase." Guo R.T., Kuo C.J., Cheng Y.S., Cheng Y.L., Liang P.H., Wang A.H.-J. Submitted (JUN-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS).
[5]	"Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures." Sun H.Y., Ko T.P., Kuo C.J., Guo R.T., Chou C.C., Liang P.H., Wang A.H. J. Bacteriol. 187:8137-8148(2005) [PubMed: 16291686] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36602.1.

PIR

C72242.

RefSeq

NP_229335.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V4E	X-ray	2.28	A/B	1-299	[»]
1V4H	X-ray	2.80	A	1-299	[»]
1V4I	X-ray	2.40	A	1-299	[»]
1V4J	X-ray	2.85	A/B	1-299	[»]
1V4K	X-ray	2.45	A	1-299	[»]
1VG2	X-ray	3.10	A	1-299	[»]
1VG3	X-ray	2.70	A	1-299	[»]
1VG4	X-ray	3.30	A/B	1-299	[»]
1VG6	X-ray	3.35	A	1-299	[»]
1VG7	X-ray	3.40	A	1-299	[»]
1WKZ	X-ray	3.40	A/B	1-299	[»]
1WL0	X-ray	3.20	A/B	1-299	[»]
1WL1	X-ray	3.45	A/B	1-299	[»]
1WL2	X-ray	2.80	A	1-299	[»]
1WL3	X-ray	3.50	A/B	1-299	[»]
2AZL	X-ray	2.80	A	1-299	[»]

ProteinModelPortal

Q9X1M1.

SMR

Q9X1M1. Positions 9-288.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897656.

GenomeReviews

Gene locus TM_1535 in contig AE000512_GR.

KEGG

tma:TM1535.

NMPDR

fig|243274.1.peg.1519.

PATRIC

23938030. VBITheMar51294_1553.

TIGR

TM_1535.

Phylogenomic databases

HOGENOM

HBG725927.

OMA

FRILANK.

PhylomeDB

Q9X1M1.

ProtClustDB

CLSK795977.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1535-MONOMER.

Family and domain databases

InterPro

IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]

Gene3D

G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.

KO

K02523.

PANTHER

PTHR12001. Polyprenyl_synt. 1 hit.

Pfam

PF00348. polyprenyl_synt. 1 hit.
[Graphical view]

SUPFAM

SSF48576. Terpenoid_synth. 1 hit.

PROSITE

PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9X1M1_THEMA

Accession

Primary (citable) accession number: Q9X1M1

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	December 14, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)