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P18079

- HEM1_RHOCB

UniProt

P18079 - HEM1_RHOCB

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Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211Substrate
Binding sitei137 – 1371Substrate
Binding sitei156 – 1561Substrate
Binding sitei189 – 1891Pyridoxal phosphate
Binding sitei217 – 2171Pyridoxal phosphate
Binding sitei245 – 2451Pyridoxal phosphate
Active sitei248 – 24811 Publication
Binding sitei277 – 2771Pyridoxal phosphate
Binding sitei278 – 2781Pyridoxal phosphate
Binding sitei365 – 3651Substrate

GO - Molecular functioni

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

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciRCAP272942:GJIY-1471-MONOMER.
RETL1328306-WGS:GSTH-5523-MONOMER.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
Ordered Locus Names:RCAP_rcc01447
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000002361: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4094095-aminolevulinate synthasePRO_0000163828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineCurated

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Beta strandi25 – 284
Beta strandi35 – 395
Beta strandi45 – 506
Helixi59 – 613
Helixi63 – 7614
Turni84 – 863
Helixi91 – 10313
Beta strandi107 – 1137
Helixi115 – 12915
Beta strandi134 – 1385
Helixi143 – 1519
Beta strandi156 – 1594
Helixi164 – 17310
Beta strandi180 – 1878
Turni189 – 1913
Helixi197 – 20711
Beta strandi210 – 2145
Turni216 – 2216
Helixi229 – 2335
Helixi236 – 2383
Beta strandi240 – 2489
Beta strandi255 – 2595
Helixi261 – 27010
Helixi272 – 2754
Helixi282 – 29514
Helixi298 – 32124
Beta strandi329 – 3313
Beta strandi333 – 3364
Helixi340 – 35415
Turni363 – 3653
Beta strandi372 – 3754
Helixi383 – 39614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BWNX-ray2.10A/B/D/E1-401[»]
2BWOX-ray2.80A/B/D/E1-401[»]
2BWPX-ray2.70A/B/D/E1-401[»]
ProteinModelPortaliP18079.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18079.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221020.
KOiK00643.
OMAiVMDSTTH.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
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.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18079 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDYNLALDKA IQKLHDEGRY RTFIDIEREK GAFPKAQWNR PDGGKQDITV
60 70 80 90 100
WCGNDYLGMG QHPVVLAAMH EALEAVGAGS GGTRNISGTT AYHRRLEAEI
110 120 130 140 150
ADLHGKEAAL VFSSAYIAND ATLSTLRVLF PGLIIYSDSL NHASMIEGIK
160 170 180 190 200
RNAGPKRIFR HNDVAHLREL IAADDPAAPK LIAFESVYSM DGDFGPIKEI
210 220 230 240 250
CDIADEFGAL TYIDEVHAVG MYGPRGAGVA ERDGLMHRID IFNGTLAKAY
260 270 280 290 300
GVFGGYIAAS AKMVDAVRSY APGFIFSTSL PPAIAAGAQA SIAFLKTAEG
310 320 330 340 350
QKLRDAQQMH AKVLKMRLKA LGMPIIDHGS HIVPVVIGDP VHTKAVSDML
360 370 380 390 400
LSDYGVYVQP INFPTVPRGT ERLRFTPSPV HDLKQIDGLV HAMDLLWARC

ALNRAEASA
Length:409
Mass (Da):44,374
Last modified:May 31, 2011 - v2
Checksum:iFCC89DA6EBA8DFB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281V → L in CAA37857. (PubMed:2381418)Curated
Sequence conflicti128 – 1281V → L in CAA37393. (PubMed:1904045)Curated
Sequence conflicti402 – 4098Missing in CAA37857. (PubMed:2381418)Curated
Sequence conflicti402 – 4098Missing in CAA37393. (PubMed:1904045)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53309 Genomic DNA. Translation: CAA37393.1.
X53864 Genomic DNA. Translation: CAA37857.1.
CP001312 Genomic DNA. Translation: ADE85192.1.
PIRiS10528.
RefSeqiYP_003577599.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE85192; ADE85192; RCAP_rcc01447.
GeneIDi9004270.
KEGGircp:RCAP_rcc01447.
PATRICi35502998. VBIRhoCap134200_1459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53309 Genomic DNA. Translation: CAA37393.1 .
X53864 Genomic DNA. Translation: CAA37857.1 .
CP001312 Genomic DNA. Translation: ADE85192.1 .
PIRi S10528.
RefSeqi YP_003577599.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BWN X-ray 2.10 A/B/D/E 1-401 [» ]
2BWO X-ray 2.80 A/B/D/E 1-401 [» ]
2BWP X-ray 2.70 A/B/D/E 1-401 [» ]
ProteinModelPortali P18079.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE85192 ; ADE85192 ; RCAP_rcc01447 .
GeneIDi 9004270.
KEGGi rcp:RCAP_rcc01447.
PATRICi 35502998. VBIRhoCap134200_1459.

Phylogenomic databases

HOGENOMi HOG000221020.
KOi K00643.
OMAi VMDSTTH.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .
BioCyci RCAP272942:GJIY-1471-MONOMER.
RETL1328306-WGS:GSTH-5523-MONOMER.

Miscellaneous databases

EvolutionaryTracei P18079.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
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.
[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. "Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a delta-aminolevulinic acid-dependent mutant strain."
    Hornberger U., Liebetanz R., Tichy H.V., Drews G.
    Mol. Gen. Genet. 221:371-378(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  2. "Use of a lacZ fusion to study transcriptional regulation of the Rhodobacter capsulatus hemA gene."
    Wright M.S., Eckert J.J., Biel S.W., Biel A.J.
    FEMS Microbiol. Lett. 62:339-342(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  3. "Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
    Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
    J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  4. "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans."
    Astner I., Schulze J.O., van den Heuvel J., Jahn D., Schubert W.D., Heinz D.W.
    EMBO J. 24:3166-3177(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-401, SUBUNIT, COFACTOR-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE.

Entry informationi

Entry nameiHEM1_RHOCB
AccessioniPrimary (citable) accession number: P18079
Secondary accession number(s): D5AT85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 31, 2011
Last modified: October 1, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3