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P13195

- HEM1_RAT

UniProt

P13195 - HEM1_RAT

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Protein

5-aminolevulinate synthase, nonspecific, mitochondrial

Gene

Alas1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191SubstrateBy similarity
Binding sitei336 – 3361SubstrateBy similarity
Binding sitei355 – 3551SubstrateBy similarity
Binding sitei388 – 3881Pyridoxal phosphateBy similarity
Binding sitei416 – 4161Pyridoxal phosphateBy similarity
Binding sitei444 – 4441Pyridoxal phosphateBy similarity
Active sitei447 – 4471By similarity
Binding sitei476 – 4761Pyridoxal phosphateBy similarity
Binding sitei477 – 4771Pyridoxal phosphateBy similarity
Binding sitei564 – 5641SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: RGD
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular response to insulin stimulus Source: RGD
  2. cellular response to organic cyclic compound Source: RGD
  3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  4. response to cAMP Source: RGD
  5. response to cobalt ion Source: RGD
  6. response to drug Source: RGD
  7. response to ethanol Source: RGD
  8. response to gonadotropin Source: RGD
  9. response to herbicide Source: RGD
  10. response to hypoxia Source: RGD
  11. response to nickel cation Source: RGD
  12. response to nutrient levels Source: RGD
  13. response to organic cyclic compound Source: RGD
  14. response to organic substance Source: RGD
  15. response to platinum ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, nonspecific, mitochondrial (EC:2.3.1.37)
Short name:
ALAS-H
Alternative name(s):
5-aminolevulinic acid synthase 1
Delta-ALA synthase 1
Delta-aminolevulinate synthase 1
Gene namesi
Name:Alas1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi68392. Alas1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: InterPro
  2. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656MitochondrionAdd
BLAST
Chaini57 – 6425865-aminolevulinate synthase, nonspecific, mitochondrialPRO_0000001232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP13195.

Expressioni

Gene expression databases

GenevestigatoriP13195.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP13195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG005954.
InParanoidiP13195.
KOiK00643.
PhylomeDBiP13195.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13195-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTVST
60 70 80 90 100
SAAQCQQVKE TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPPGHPSP
110 120 130 140 150
STSQSSGSKC PFLAAQLSQT GSSVFRKASL ELQEDVQEMH AVRKEVAQSP
160 170 180 190 200
VLPSLVNAKR DGEGPSPLLK NFQDIMRKQR PERVSHLLQD NLPKSVSTFQ
210 220 230 240 250
YDHFFEKKID EKKNDHTYRV FKTVNRRAQI FPMADDYTDS LITKKQVSVW
260 270 280 290 300
CSNDYLGMSR HPRVCGAVIE TVKQHGAGAG GTRNISGTSK FHVELEQELA
310 320 330 340 350
DLHGKDAALL FSSCFVANDS TLFTLAKMMP GCEIYSDSGN HASMIQGIRN
360 370 380 390 400
SRVPKYIFRH NDVNHLRELL QRSDPSVPKI VAFETVHSMD GAVCPLEELC
410 420 430 440 450
DVAHEFGAIT FVDEVHAVGL YGASGGGIGD RDGVMPKMDI ISGTLGKAFG
460 470 480 490 500
CVGGYIASTS LLIDTVRSYA AGFIFTTSLP PMLLAGALES VRILKSNEGR
510 520 530 540 550
ALRRQHQRNV KLMRQMLMDA GLPVIHCPSH IIPVRVADAA KNTEICDELM
560 570 580 590 600
TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFLE KLLLTWKRVG
610 620 630 640
LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA
Length:642
Mass (Da):71,021
Last modified:September 27, 2004 - v2
Checksum:iB28FC05D5F834886
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 13619SQTGS…LQEDV → ARRAAASSARPVWSFRRTW in AAA40790. (PubMed:3356687)CuratedAdd
BLAST
Sequence conflicti144 – 1441K → T in AAA40790. (PubMed:3356687)Curated
Sequence conflicti195 – 1951S → V in AAA40790. (PubMed:3356687)Curated
Sequence conflicti244 – 2452KK → NN in AAA40790. (PubMed:3356687)Curated
Sequence conflicti251 – 2511C → S in AAA40790. (PubMed:3356687)Curated
Sequence conflicti377 – 3771V → L in AAA40724. (PubMed:3182776)Curated
Sequence conflicti587 – 5871F → Y in AAA40790. (PubMed:3356687)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03190 mRNA. Translation: AAA40790.1.
J04044 mRNA. Translation: AAA40724.1.
BC061793 mRNA. Translation: AAH61793.1.
PIRiA28191. SYRTAL.
RefSeqiNP_077810.2. NM_024484.2.
UniGeneiRn.97126.

Genome annotation databases

GeneIDi65155.
KEGGirno:65155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03190 mRNA. Translation: AAA40790.1 .
J04044 mRNA. Translation: AAA40724.1 .
BC061793 mRNA. Translation: AAH61793.1 .
PIRi A28191. SYRTAL.
RefSeqi NP_077810.2. NM_024484.2.
UniGenei Rn.97126.

3D structure databases

ProteinModelPortali P13195.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P13195.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65155.
KEGGi rno:65155.

Organism-specific databases

CTDi 211.
RGDi 68392. Alas1.

Phylogenomic databases

HOVERGENi HBG005954.
InParanoidi P13195.
KOi K00643.
PhylomeDBi P13195.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .

Miscellaneous databases

NextBioi 614001.
PROi P13195.

Gene expression databases

Genevestigatori P13195.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 2 hits.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01821. 5aminolev_synth. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.

Entry informationi

Entry nameiHEM1_RAT
AccessioniPrimary (citable) accession number: P13195
Secondary accession number(s): Q6P782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: September 27, 2004
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3