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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciPAES290512:GHUT-201-MONOMER.
UniPathwayiUPA00251; UER00317.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:Paes_0193
OrganismiProsthecochloris aestuarii (strain DSM 271 / SK 413)
Taxonomic identifieri290512 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris
ProteomesiUP000002725: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290512.Paes_0193.

Structurei

3D structure databases

ProteinModelPortaliB4S3Q6.
SMRiB4S3Q6. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4S3Q6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQLTRSAEL FEKAKQFIPG GVNSPVRAFK SVGGTPIYMA KGQGAYMTDV
60 70 80 90 100
DGNTYLDYVG SWGPFILGSM HPRITAALEH TLTKIGTSFG TPIEMEIEIA
110 120 130 140 150
ELLCQIVPSI EMVRMVNSGT EATMSAVRLA RGYTSRDKII KFEGCYHGHG
160 170 180 190 200
DSFLIKAGSG ALTLGAPDSP GVTKGTANDT LNAKYNDIES VRLLVNENKG
210 220 230 240 250
NIAAIIIEPV AGNTGVIPAK PGFLQALRDL CTEEGIVLIF DEVMCGFRVA
260 270 280 290 300
LGGAQERYGV TPDLTTMGKI IGGGLPVGAF GGKREIMERI APLGDVYQAG
310 320 330 340 350
TLSGNPLALT AGLETLKILR DENPYPELER KAAFLEEGFR NNMNKLGLNY
360 370 380 390 400
VQNRVGSMAC LFFTETPVTD YDTAVTADLK KYGTYYHAML DQGIYLAPSQ
410 420 430
FEAMFTSAVM TDEDLEKTVK ANYVALQATQ K
Length:431
Mass (Da):46,492
Last modified:September 23, 2008 - v1
Checksum:i777B9EED8C8A825B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF45252.1.
RefSeqiWP_012504789.1. NC_011059.1.
YP_002014899.1. NC_011059.1.

Genome annotation databases

EnsemblBacteriaiACF45252; ACF45252; Paes_0193.
GeneIDi6460269.
KEGGipaa:Paes_0193.
PATRICi23039992. VBIProAes37017_0200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF45252.1.
RefSeqiWP_012504789.1. NC_011059.1.
YP_002014899.1. NC_011059.1.

3D structure databases

ProteinModelPortaliB4S3Q6.
SMRiB4S3Q6. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290512.Paes_0193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF45252; ACF45252; Paes_0193.
GeneIDi6460269.
KEGGipaa:Paes_0193.
PATRICi23039992. VBIProAes37017_0200.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciPAES290512:GHUT-201-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 271 / SK 413.

Entry informationi

Entry nameiGSA_PROA2
AccessioniPrimary (citable) accession number: B4S3Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: February 4, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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 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.