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C6AR33

- GSA_TERTT

UniProt

C6AR33 - GSA_TERTT

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene
hemL, TERTU_3069
Organism
Teredinibacter turnerae (strain ATCC 39867 / T7901)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate By similarity.UniRule 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. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciTTUR377629:GHSU-2786-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Ordered Locus Names:TERTU_3069
OrganismiTeredinibacter turnerae (strain ATCC 39867 / T7901)
Taxonomic identifieri377629 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadales genera incertae sedisTeredinibacter
ProteomesiUP000009080: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotationPRO_1000205646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi377629.TERTU_3069.

Structurei

3D structure databases

ProteinModelPortaliC6AR33.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiRAIKPYP.
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.

C6AR33-1 [UniParc]FASTAAdd to Basket

« Hide

MSNFSEVFAR AQKTIPGGVN SPVRAFKAVG GEPVFIDHAK GAYVYDIHGK    50
RYVDYVLSWG PMLLGHGDDD VLDAVRAKLD KGLSFGAPTE IETELAEKIC 100
NIMPGMDKVR FVNSGTEATM SAIRLARGYT GRDKIVKFEG CYHGHSDSLL 150
IKAGSGALTL GVPSSPGVPA CLAEHTITLT YNNIEQVRQL FRDRGNEIAC 200
IIVEPVAGNM NCIPPEPGFL QALREVCTQA DALLIFDEVM TGFRLGLSGA 250
QGYYQVQPDI TTLGKVIGGG MPVGAFGGSE RIMDFIAPVG PVYQAGTLSG 300
NPVAMAAGLK TLEKISAEGF YQPIFDKTAA LCRNLESAAK EAGIGFTTNY 350
VGSMWGGFFT EEEKISNYQQ VMACNTERFN RFFHGMLDEG VYLAPASYEA 400
GFMSVSHSDE DIDFTVNAAR KVFANIK 427
Length:427
Mass (Da):46,046
Last modified:September 1, 2009 - v1
Checksum:iA53FD6A4FA7BA1AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001614 Genomic DNA. Translation: ACS93577.1.
RefSeqiYP_003074446.1. NC_012997.1.

Genome annotation databases

EnsemblBacteriaiACS93577; ACS93577; TERTU_3069.
GeneIDi8213987.
KEGGittu:TERTU_3069.
PATRICi23873053. VBITerTur118718_2853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001614 Genomic DNA. Translation: ACS93577.1 .
RefSeqi YP_003074446.1. NC_012997.1.

3D structure databases

ProteinModelPortali C6AR33.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 377629.TERTU_3069.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACS93577 ; ACS93577 ; TERTU_3069 .
GeneIDi 8213987.
KEGGi ttu:TERTU_3069.
PATRICi 23873053. VBITerTur118718_2853.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OMAi RAIKPYP.
OrthoDBi EOG6QVRHN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci TTUR377629:GHSU-2786-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPi MF_00375. HemL_aminotrans_3.
InterProi IPR004639. 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 ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00713. hemL. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39867 / T7901.

Entry informationi

Entry nameiGSA_TERTT
AccessioniPrimary (citable) accession number: C6AR33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 37 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

Documents

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

External Data

Dasty 3

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