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Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from glycine.
Proteins known to be involved in this subpathway in this organism are:
  1. 5-aminolevulinate synthase (hemA)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from glycine, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21Substrate1 Publication1
Binding sitei137Substrate1 Publication1
Binding sitei156Substrate1 Publication1
Binding sitei189Pyridoxal phosphate1 Publication1
Binding sitei217Pyridoxal phosphate1 Publication1
Binding sitei245Pyridoxal phosphate1 Publication1
Active sitei2481 Publication1
Binding sitei277Pyridoxal phosphate; shared with dimeric partner1 Publication1
Binding sitei278Pyridoxal phosphate; shared with dimeric partner1 Publication1
Binding sitei365Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.3.1.37. 5381.
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
Proteomesi
  • UP000002361 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001638281 – 4095-aminolevulinate synthaseAdd BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei248N6-(pyridoxal phosphate)lysineCurated1

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi272942.RCAP_rcc01447.

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 16Combined sources14
Beta strandi25 – 28Combined sources4
Beta strandi35 – 39Combined sources5
Beta strandi45 – 50Combined sources6
Helixi59 – 61Combined sources3
Helixi63 – 76Combined sources14
Turni84 – 86Combined sources3
Helixi91 – 103Combined sources13
Beta strandi107 – 113Combined sources7
Helixi115 – 129Combined sources15
Beta strandi134 – 138Combined sources5
Helixi143 – 151Combined sources9
Beta strandi156 – 159Combined sources4
Helixi164 – 173Combined sources10
Beta strandi180 – 187Combined sources8
Turni189 – 191Combined sources3
Helixi197 – 207Combined sources11
Beta strandi210 – 214Combined sources5
Turni216 – 221Combined sources6
Helixi229 – 233Combined sources5
Helixi236 – 238Combined sources3
Beta strandi240 – 248Combined sources9
Beta strandi255 – 259Combined sources5
Helixi261 – 270Combined sources10
Helixi272 – 275Combined sources4
Helixi282 – 295Combined sources14
Helixi298 – 321Combined sources24
Beta strandi329 – 331Combined sources3
Beta strandi333 – 336Combined sources4
Helixi340 – 354Combined sources15
Turni363 – 365Combined sources3
Beta strandi372 – 375Combined sources4
Helixi383 – 396Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP18079.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18079.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107EEK. Bacteria.
COG0156. LUCA.
HOGENOMiHOG000221020.
KOiK00643.
OMAiKEITVWC.
OrthoDBiPOG091H024U.

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.

P18079-1 [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)DescriptionActionsGraphical viewLength
Sequence conflicti128V → L in CAA37857 (PubMed:2381418).Curated1
Sequence conflicti128V → L in CAA37393 (PubMed:1904045).Curated1
Sequence conflicti402 – 409Missing in CAA37857 (PubMed:2381418).Curated8
Sequence conflicti402 – 409Missing in CAA37393 (PubMed:1904045).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53309 Genomic DNA. Translation: CAA37393.1.
X53864 Genomic DNA. Translation: CAA37857.1.
CP001312 Genomic DNA. Translation: ADE85192.1.
PIRiS10528.
RefSeqiWP_013067171.1. NC_014034.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53309 Genomic DNA. Translation: CAA37393.1.
X53864 Genomic DNA. Translation: CAA37857.1.
CP001312 Genomic DNA. Translation: ADE85192.1.
PIRiS10528.
RefSeqiWP_013067171.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP18079.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc01447.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107EEK. Bacteria.
COG0156. LUCA.
HOGENOMiHOG000221020.
KOiK00643.
OMAiKEITVWC.
OrthoDBiPOG091H024U.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.
BRENDAi2.3.1.37. 5381.

Miscellaneous databases

EvolutionaryTraceiP18079.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.