O52552 (O52552_AMYMD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
RifK EMBL AAC01720.1

Gene names

Name:

rifK EMBL AAC01720.1

Organism

Amycolatopsis mediterranei (Nocardia mediterranei) EMBL AAC01720.1

Taxonomic identifier

33910 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the degT/dnrJ/eryC1 family. RuleBase RU004508

Ontologies

Keywords
Ligand	Pyridoxal phosphate RuleBase RU004508
Technical term	3D-structure PDB 1B9H PDB 1B9I
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Molecular_function	catalytic activity Inferred from electronic annotation. Source: InterPro pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Site	88	1	Important for catalytic activity PDB 1B9H
	Site	159	1	Important for catalytic activity PDB 1B9H
	Site	188	1	Important for catalytic activity PDB 1B9H
Amino acid modifications
	Modified residue	188	1	N6-(pyridoxal phosphate)lysine PDB 1B9H

Sequences

	Sequence		Length	Mass (Da)
	O52552 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 6657B4F41F641190	FASTA	388	42,138
	10 20 30 40 50 60 MNARKAPEFP AWPQYDDAER NGLVRALEQG QWWRMGGDEV NSFEREFAAH HGAAHALAVT 70 80 90 100 110 120 NGTHALELAL QVMGVGPGTE VIVPAFTFIS SSQAAQRLGA VTVPVDVDAA TYNLDPEAVA 130 140 150 160 170 180 AAVTPRTKVI MPVHMAGLMA DMDALAKISA DTGVPLLQDA AHAHGARWQG KRVGELDSIA 190 200 210 220 230 240 TFSFQNGKLM TAGEGGAVVF PDGETEKYET AFLRHSCGRP RDDRRYFHKI AGSNMRLNEF 250 260 270 280 290 300 SASVLRAQLA RLDEQIAVRD EPWTLLSRLL GAIDGVVPQG GDVRADRNSH YMAMFRIPGL 310 320 330 340 350 360 TEERRNALVD RLVEAGLPAF AAFRAIYRTD AFWELGAPDE SVDAIARRCP NTDAISSDCV 370 380 WLHHRVLLAG EPELHATAEI IADAVGRA

References

[1]	"Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699." August P.R., Tang L., Yoon Y.J., Ning S., Muller R., Yu T.W., Taylor M., Hoffmann D., Kim C.G., Zhang X., Hutchinson C.R., Floss H.G. Chem. Biol. 5:69-79(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01720.1.
[2]	"3-amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics." Kim C.G., Yu T.W., Fryhle C.B., Handa S., Floss H.G. J. Biol. Chem. 273:6030-6040(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01720.1.
[3]	"Rifamycin insusceptibility: exploring the rif gene cluster of Amycolatopsis mediterranei S699." Yu T.-W., Pogosova-Agadjanyan E.L., Kuan L.-Y., Bai L., Tin A.M., Adman E., Floss H.G. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01720.1.
[4]	"Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase." Eads J.C., Beeby M., Scapin G., Yu T.W., Floss H.G. Biochemistry 38:9840-9849(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 5-388, ACTIVE SITE, AND PYRIDOXAL PHOSPHATE AT LYS-188.
[5]	"Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in amycolatopsis Mediterranei S699." Yu T.W., Muller R., Muller M., Zhang X., Draeger G., Kim C.G., Leistner E., Floss H.G. J. Biol. Chem. 276:12546-12555(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01720.1.
[6]	Yu T., August P.R., Tang L., Yoon Y.J., Ning S., Mueller R., Taylor M., Kim C., Zhang X., Pogosova-Agadjanyan E.L., Tin A.M., Hutchinson C.R., Floss H.G. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: S699 EMBL AAC01720.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF040570 Genomic DNA. Translation: AAC01720.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B9H	X-ray	2.00	A	1-388	[»]
1B9I	X-ray	2.00	A	5-388	[»]

ProteinModelPortal

O52552.

SMR

O52552. Positions 5-388.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14078.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]

PIRSF

PIRSF000390. PLP_StrS. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O52552.

Entry information

Entry name

O52552_AMYMD

Accession

Primary (citable) accession number: O52552

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 1998
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)