Q5Z8V9 (HEM2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-aminolevulinic acid dehydratase, chloroplastic
Short name=ALADH
EC=4.2.1.24

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	HEMB
Ordered Locus Names:	Os06g0704600, LOC_Os06g49110
ORF Names:	P0018H04.2, OsJ_22561

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen By similarity.
Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O.
Cofactor	Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer By similarity.
Subcellular location	Plastid › chloroplast Probable.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Heme biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 45	45	Chloroplast Potential
	Chain	46 – 426	381	Delta-aminolevulinic acid dehydratase, chloroplastic		PRO_0000376065
Sites
	Active site	293	1	Schiff-base intermediate with substrate By similarity
	Active site	346	1	Schiff-base intermediate with substrate By similarity
	Metal binding	331	1	Magnesium By similarity
	Binding site	303	1	Substrate 1 By similarity
	Binding site	315	1	Substrate 1 By similarity
	Binding site	372	1	Substrate 2 By similarity
	Binding site	411	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5Z8V9 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 04A43F6AE5E51DAF	FASTA	426	46,286
	10 20 30 40 50 60 MASTVSFSPA NVQMLQGRSC HGHAAFGGCS AVPRTGPRMR SVAVRVSSEQ EAAPAVRAPS 70 80 90 100 110 120 GRTIEECEAD AVAGRFPAPP PLVRPKAPEG TPQIRPLDLT KRPRRNRRSP ALRAAFQETT 130 140 150 160 170 180 ISPANLVLPL FIHEGEDDAP IGAMPGCYRL GWRHGLLDEV YKSRDVGVNS FVLFPKVPDA 190 200 210 220 230 240 LKSQSGDEAY NDNGLVPRTI RLLKDKFPDI VVYTDVALDP YSSDGHDGIV REDGVIMNDE 250 260 270 280 290 300 TVYQLCKQAV SQARAGADVV SPSDMMDGRV GAIRAALDAE GFHDVSIMSY TAKYASSFYG 310 320 330 340 350 360 PFREALDSNP RFGDKKTYQM NPANYREALL ETAADEAEGA DILLVKPGLP YLDVIRLLRD 370 380 390 400 410 420 NSALPIAAYQ VSGEYSMIKA GGALNMIDEE KVMMESLMCL RRAGADIILT YFARQAANVL CGMRSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[2]	"The rice annotation project database (RAP-DB): 2008 update." The rice annotation project (RAP) Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed: 18089549] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[3]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[4]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP003761 Genomic DNA. Translation: BAD53795.1. AP008212 Genomic DNA. Translation: BAF20424.1. CM000143 Genomic DNA. Translation: EAZ38208.1. AK065784 mRNA. Translation: BAG89678.1. AK119551 mRNA. Translation: BAG99687.1.
RefSeq	NP_001058510.1. NM_001065045.1.
UniGene	Os.7836.
3D structure databases
HSSP	HSSP built from PDB template 1PV8 based on UniProtKB P13716.
ProteinModelPortal	Q5Z8V9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5Z8V9.
Proteomic databases
PRIDE	Q5Z8V9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os06g49110.1; LOC_Os06g49110.1; LOC_Os06g49110. LOC_Os06g49110.3; LOC_Os06g49110.3; LOC_Os06g49110.
GeneID	4341997.
KEGG	osa:4341997.
Organism-specific databases
Gramene	Q5Z8V9.
Phylogenomic databases
GeneTree	EPGT00050000017638.
HOGENOM	HBG285270.
OMA	FTSHGHD.
PhylomeDB	Q5Z8V9.
ProtClustDB	CLSN2679842.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_ORYSJ

Accession

Primary (citable) accession number: Q5Z8V9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program