Q9S4T0 (HGD_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Homogentisate 1,2-dioxygenase
EC=1.13.11.5

Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase

Gene names

Name:	hmgA
Ordered Locus Names:	lpg1285

Organism

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]

Taxonomic identifier

272624 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella › Legionella pneumophila › Legionella pneumophila subsp. pneumophila

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Homogentisate + O2 = 4-maleylacetoacetate. HAMAP-Rule MF_00334
Cofactor	Iron By similarity.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6. HAMAP-Rule MF_00334
Sequence similarities	Belongs to the homogentisate dioxygenase family.
Sequence caution	The sequence AAD51397.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: HAMAP tyrosine catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	homogentisate 1,2-dioxygenase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 416	416	Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334		PRO_0000220248
Sites
	Metal binding	318	1	Iron By similarity
	Metal binding	324	1	Iron By similarity
	Metal binding	354	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S4T0 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 9E06F5AB9FFF3C9B	FASTA	416	47,475
	10 20 30 40 50 60 MYLQGFGNYH HSEAVKGALP PNQNSPQHCS LGLYAEQLSG TAFTRPRHNN LRSWLYRILP 70 80 90 100 110 120 TVTQGTYYPY EFNIMQPFVD ELSPNAMRWS PLYNSSQIKC DFVEGLFHIA GSPLVNTYTY 130 140 150 160 170 180 YCNHSMSDKY FANNDGELLF VPYAGEIHLH TEFGKLMLSS GSIAVIPRGV KFKVEVISKE 190 200 210 220 230 240 AKGYLCENSG NPLTLPQLGP IGANGLANPR HFQYPVAAFE NSGSEHTIIC KNQKKLWFTV 250 260 270 280 290 300 CNHSPLNVVA WHGNYAPYCY DLSLFNTINT VSFDHPDPSI FTVLTSESEI PGVSNLDFVI 310 320 330 340 350 360 FPPRWMVAEH TFRPPYFHRN YMNELMGLVY GEYDAKKEGF IPGGISIHNC MTPHGPDYES 370 380 390 400 410 YEIAASQDLK PNYINSLAFM FETKDYWQVT EQAYRHPSRQ MDYLNCWQGF KIEFSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Legionella pneumophila rpoS gene is required for growth within Acanthamoeba castellanii." Hales L.M., Shuman H.A. J. Bacteriol. 181:4879-4889(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genomic sequence of the accidental pathogen Legionella pneumophila." Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J. Science 305:1966-1968(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF117715 Genomic DNA. Translation: AAD51397.1. Different initiation. AE017354 Genomic DNA. Translation: AAU27368.1.
RefSeq	YP_095315.1. NC_002942.5.
3D structure databases
ProteinModelPortal	Q9S4T0.
ModBase	Search...
Protein-protein interaction databases
STRING	272624.lpg1285.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU27368; AAU27368; lpg1285.
GeneID	3080383.
KEGG	lpn:lpg1285.
PATRIC	22329658. VBILegPne29832_1353.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3508.
HOGENOM	HOG000139824.
KO	K00451.
OMA	AVTKWGL.
ProtClustDB	PRK05341.
Enzyme and pathway databases
BioCyc	LPNE272624:GHDI-1320-MONOMER.
UniPathway	UPA00139; UER00339.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
HAMAP	MF_00334. Homogentis_dioxygen.
InterPro	IPR005708. Homogentis_dOase. IPR022950. Homogentis_dOase_bac. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR11056. PTHR11056. 1 hit.
Pfam	PF04209. HgmA. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR01015. hmgA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HGD_LEGPH

Accession

Primary (citable) accession number: Q9S4T0
Secondary accession number(s): Q5ZW03

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program