P13195 (HEM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5-aminolevulinate synthase, nonspecific, mitochondrial
Short name=ALAS-H
EC=2.3.1.37

Alternative name(s):
5-aminolevulinic acid synthase 1
Delta-ALA synthase 1
Delta-aminolevulinate synthase 1

Gene names

Name:

Alas1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	642 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)

Catalytic activity	Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.
Cofactor	Pyridoxal phosphate.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion matrix.
Miscellaneous	There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to insulin stimulus Inferred from expression pattern. Source: RGD cellular response to organic cyclic compound Inferred from expression pattern. Source: RGD heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to cAMP Inferred from expression pattern. Source: RGD response to cobalt ion Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to ethanol Inferred from expression pattern. Source: RGD response to gonadotropin stimulus Inferred from expression pattern. Source: RGD response to herbicide Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to nickel cation Inferred from expression pattern. Source: RGD response to nutrient levels Inferred from expression pattern. Source: RGD response to platinum ion Inferred from expression pattern. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5-aminolevulinate synthase activity Inferred from direct assay Ref.2. Source: RGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 56	56	Mitochondrion
	Chain	57 – 642	586	5-aminolevulinate synthase, nonspecific, mitochondrial		PRO_0000001232
Amino acid modifications
	Modified residue	447	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	118 – 136	19	SQTGS…LQEDV → ARRAAASSARPVWSFRRTW in AAA40790. Ref.1
	Sequence conflict	144	1	K → T in AAA40790. Ref.1
	Sequence conflict	195	1	S → V in AAA40790. Ref.1
	Sequence conflict	244 – 245	2	KK → NN in AAA40790. Ref.1
	Sequence conflict	251	1	C → S in AAA40790. Ref.1
	Sequence conflict	377	1	V → L in AAA40724. Ref.2
	Sequence conflict	587	1	F → Y in AAA40790. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13195 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: B28FC05D5F834886	FASTA	642	71,021
	10 20 30 40 50 60 METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTVST SAAQCQQVKE 70 80 90 100 110 120 TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPPGHPSP STSQSSGSKC PFLAAQLSQT 130 140 150 160 170 180 GSSVFRKASL ELQEDVQEMH AVRKEVAQSP VLPSLVNAKR DGEGPSPLLK NFQDIMRKQR 190 200 210 220 230 240 PERVSHLLQD NLPKSVSTFQ YDHFFEKKID EKKNDHTYRV FKTVNRRAQI FPMADDYTDS 250 260 270 280 290 300 LITKKQVSVW CSNDYLGMSR HPRVCGAVIE TVKQHGAGAG GTRNISGTSK FHVELEQELA 310 320 330 340 350 360 DLHGKDAALL FSSCFVANDS TLFTLAKMMP GCEIYSDSGN HASMIQGIRN SRVPKYIFRH 370 380 390 400 410 420 NDVNHLRELL QRSDPSVPKI VAFETVHSMD GAVCPLEELC DVAHEFGAIT FVDEVHAVGL 430 440 450 460 470 480 YGASGGGIGD RDGVMPKMDI ISGTLGKAFG CVGGYIASTS LLIDTVRSYA AGFIFTTSLP 490 500 510 520 530 540 PMLLAGALES VRILKSNEGR ALRRQHQRNV KLMRQMLMDA GLPVIHCPSH IIPVRVADAA 550 560 570 580 590 600 KNTEICDELM TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFLE KLLLTWKRVG 610 620 630 640 LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of 5-aminolevulinate synthase mRNA in different rat tissues." Srivastava G., Borthwick I.A., Maguire D.J., Elferink C.J., Bawden M.J., Mercer J.F.B., May B.K. J. Biol. Chem. 263:5202-5209(1988) [PubMed: 3356687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structure, turnover, and heme-mediated suppression of the level of mRNA encoding rat liver delta-aminolevulinate synthase." Yamamoto M., Kure S., Engel J.D., Hiraga K. J. Biol. Chem. 263:15973-15979(1988) [PubMed: 3182776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03190 mRNA. Translation: AAA40790.1. J04044 mRNA. Translation: AAA40724.1. BC061793 mRNA. Translation: AAH61793.1.
IPI	IPI00198584.
PIR	SYRTAL. A28191.
RefSeq	NP_077810.2. NM_024484.2.
UniGene	Rn.97126.
3D structure databases
ProteinModelPortal	P13195.
ModBase	Search...
Proteomic databases
PRIDE	P13195.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	65155.
KEGG	rno:65155.
Organism-specific databases
CTD	211.
RGD	68392. Alas1.
Phylogenomic databases
eggNOG	maNOG04256.
HOVERGEN	HBG005954.
PhylomeDB	P13195.
Gene expression databases
Genevestigator	P13195.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR015118. 5aminolev_synth_preseq. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00643.
Pfam	PF00155. Aminotran_1_2. 1 hit. PF09029. Preseq_ALAS. 2 hits. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	614001.

Entry information

Entry name

HEM1_RAT

Accession

Primary (citable) accession number: P13195
Secondary accession number(s): Q6P782

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	September 27, 2004
Last modified:	November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program