Q9X4F5 (HGD_RHIME) 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:	R02939
ORF Names:	SMc03208

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium › Rhizobium meliloti

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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
Induction	By nitrogen and carbon deprivation as well as in the presence of tyrosine. Also induced by phenylalanine, but only in nitrogen-free medium. HAMAP-Rule MF_00334
Sequence similarities	Belongs to the homogentisate dioxygenase family.

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 – 453	453	Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334		PRO_0000220254
Sites
	Metal binding	349	1	Iron By similarity
	Metal binding	355	1	Iron By similarity
	Metal binding	385	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X4F5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: AC49AEFF0C783200	FASTA	453	50,756
	10 20 30 40 50 60 MLEKAEKQRR AGSGQQRAAG YMPGFGNDFE TESLPGALPQ GQNSPQKCNY GLYAEQLSGS 70 80 90 100 110 120 PFTAPRGTNE RSWLYRIRPS VRHTGRFRRV DYPHWKTAPH VGEHSLALGQ LRWSPLPAPS 130 140 150 160 170 180 EALDFLQGIR TMTTAGDALT QAGMAAHAYA FNADMVDDYF FNADGELLIV PETGAIQVFT 190 200 210 220 230 240 ELGRMDVEPS EICLIPRGMM FKVTRLGEEK VWRGYICENY GAKFTLPDRG PIGANCLANP 250 260 270 280 290 300 RDFKTPVAAY EDKETPCRVQ VKWCGSFHMV EIGHSPLDVV AWHGNYAPYK YDLKTFSPVG 310 320 330 340 350 360 AILFDHPDPS IFTVLTAPSG EEGTANVDFV IFPPRWLVAE HTFRPPWYHR NIMSEFMGLI 370 380 390 400 410 420 YGRYDAKEEG FVPGGMSLHN MMLAHGPDFS GFEKASNGEL KPVKLDNTMA FMFETRFPQQ 430 440 450 LTTFAAELDT LQDDYMDCWS GLERKFDGTP GIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine." Milcamps A., de Bruijn F.J. Microbiology 145:935-947(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1021.
[2]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[3]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF109131 Genomic DNA. Translation: AAD29874.1. AL591688 Genomic DNA. Translation: CAC47518.1.
RefSeq	NP_387045.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q9X4F5.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMc03208.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC47518; CAC47518; SMc03208.
GeneID	1234616.
KEGG	sme:SMc03208.
PATRIC	23635464. VBISinMel96828_4461.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3508.
HOGENOM	HOG000139824.
KO	K00451.
OMA	AVTKWGL.
ProtClustDB	PRK05341.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-3008-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_RHIME

Accession

Primary (citable) accession number: Q9X4F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program