Q45135 (Q45135_9MICO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Homoprotocatechuate 2,3-dioxygenase EMBL AAB66502.1
Organism	Brevibacterium fuscum EMBL AAB66502.1
Taxonomic identifier	47914 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Brevibacteriaceae › Brevibacterium

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3BZA PDB 3OJT PDB 3OJJ PDB 3OJN PDB 3OJK Iron PDB 1Q0C PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJT Metal-binding PDB 1Q0C PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3BZA PDB 3OJT PDB 3OJJ PDB 3OJN PDB 3OJK
Molecular function	Dioxygenase EMBL AAB66502.1 Oxidoreductase
Technical term	3D-structure PDB 1Q0C PDB 1F1X PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3BZA PDB 3OJT PDB 3OJJ PDB 3OJN PDB 3OJK
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	155	1	Iron; via tele nitrogen PDB 1Q0C PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJT
	Metal binding	184	1	Calcium PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJJ
	Metal binding	185	1	Calcium PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJJ
	Metal binding	214	1	Iron; via tele nitrogen PDB 1Q0C PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJT
	Metal binding	267	1	Iron PDB 1Q0C PDB 1Q0O PDB 2IG9 PDB 2IGA PDB 3ECJ PDB 3ECK PDB 3OJT

Sequences

	Sequence		Length	Mass (Da)
	Q45135 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 2B589C989665BAC1	FASTA	365	41,699
	10 20 30 40 50 60 MSNEIPKPVA PAPDILRCAY AELVVTDLAK SRNFYVDVLG LHVSYEDENQ IYLRSFEEFI 70 80 90 100 110 120 HHNLVLTKGP VAALKAMAFR VRTPEDVDKA EAYYQELGCR TERRKDGFVK GIGDALRVED 130 140 150 160 170 180 PLGFPYEFFF ETTHVERLHM RYDLYSAGEL VRLDHFNQVT PDVPRGRKYL EDLGFRVTED 190 200 210 220 230 240 IQDDEGTTYA AWMHRKGTVH DTALTGGNGP RLHHVAFSTH EKHNIIQICD KMGALRISDR 250 260 270 280 290 300 IERGPGRHGV SNAFYLYILD PDNHRIEIYT QDYYTGDPDN PTITWNVHDN QRRDWWGNPV 310 320 330 340 350 360 VPSWYTEASK VLDLDGNVQE IIERTDDSEL EVTIGADGFS FTRAGDEDGS YHGQASKGFK LGNQL

References

[1]	"Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum." Wang Y.Z., Lipscomb J.D. Protein Expr. Purif. 10:1-9(1997) [PubMed: 9179284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 15993 EMBL AAB66502.1.
[2]	Wang Y.-Z. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 15993 EMBL AAB66502.1.
[3]	"Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases." Vetting M.W., Wackett L.P., Que L. Jr, Lipscomb J.D., Ohlendorf D.H. J. Bacteriol. 186:1945-1958(2004) [PubMed: 15028678] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-322 IN COMPLEX WITH IRON.
[4]	"Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state." Emerson J.P., Kovaleva E.G., Farquhar E.R., Lipscomb J.D., Que L. Proc. Natl. Acad. Sci. U.S.A. 105:7347-7352(2008) [PubMed: 18492808] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
[5]	"Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates." Kovaleva E.G., Lipscomb J.D. Science 316:453-457(2007) [PubMed: 17446402] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CALCIUM AND IRON.
[6]	"Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase." Kovaleva E.G., Lipscomb J.D. Biochemistry 47:11168-11170(2008) [PubMed: 18826259] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH CALCIUM AND IRON.
[7]	"A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase." Fielding A.J., Kovaleva E.G., Farquhar E.R., Lipscomb J.D., Que L. J. Biol. Inorg. Chem. 16:341-355(2011) [PubMed: 21153851] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CALCIUM AND IRON.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U58132 Genomic DNA. Translation: AAB66502.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F1X	X-ray	1.60	A/B/C/D	1-322	[»]
1Q0C	X-ray	2.10	A/B/C/D	1-365	[»]
1Q0O	X-ray	2.30	A/B	1-365	[»]
2IG9	X-ray	1.90	A/B/C/D	1-365	[»]
2IGA	X-ray	1.95	A/B/C/D	1-365	[»]
3BZA	X-ray	1.70	A/B/C/D	1-365	[»]
3ECJ	X-ray	1.65	A/B/C/D	1-365	[»]
3ECK	X-ray	1.60	A/B/C/D	1-365	[»]
3OJJ	X-ray	1.72	A/B/C/D	1-365	[»]
3OJK	X-ray	1.68	A/B/C/D	1-365	[»]
3OJN	X-ray	1.65	A/B/C/D	1-365	[»]
3OJT	X-ray	1.70	A/B/C/D	1-365	[»]

ProteinModelPortal

Q45135.

SMR

Q45135. Positions 4-362.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR011981. dHPA_dOase.
IPR004360. Glyas_Fos-R_dOase.
[Graphical view]

Pfam

PF00903. Glyoxalase. 2 hits.
[Graphical view]

TIGRFAMs

TIGR02295. HpaD. 1 hit.

ProtoNet

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Entry information

Entry name

Q45135_9MICO

Accession

Primary (citable) accession number: Q45135

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)