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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
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

BioCyciPMAR59919:GJMQ-503-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:PMM0483
OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Taxonomic identifieri59919 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001026: 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi59919.PMM0483.

Structurei

3D structure databases

ProteinModelPortaliQ7V2J3.
SMRiQ7V2J3. Positions 5-423.
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.

Q7V2J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDILKTTYS EEVFSSALEL MPGGVSSPVR AFKSVGGQPI VFDRVKGPYA
60 70 80 90 100
WDIDGNRYID YIGSWGPAIC GHAHPEVITA LQEAIEKGTS FGAPCVLENK
110 120 130 140 150
LAEMVIDAVP SVEMVRFVNS GTEACMAVLR LMRAFTGRDK VIKFDGCYHG
160 170 180 190 200
HADMFLVKAG SGVATLGLPD SPGVPRTTTA NTLTAPYNDL EAVKKLFSEN
210 220 230 240 250
PDAISGVILE PIVGNAGFIT PEPGFLEGLR ELTTENGSLL VFDEVMTGFR
260 270 280 290 300
ISYGGAQEKF GVTPDLTTLG KVIGGGLPVG AYGGKKEIMS MVAPSGPVYQ
310 320 330 340 350
AGTLSGNPLA MTAGIKTLEL LKQEGTYEKL ESTTSRLIEG IIQSAENNGI
360 370 380 390 400
AINGGSVSAM FGFFLCEGPV RNFEEAKTNN SELFGKLHRE MLKRGVYLAP
410 420 430
SPFEAGFTSL AHSEEEIDRT LEAFDQSFSV IKN
Length:433
Mass (Da):46,265
Last modified:October 1, 2003 - v1
Checksum:i6222CFA0204B37B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548174 Genomic DNA. Translation: CAE18942.1.
RefSeqiNP_892601.1. NC_005072.1.
WP_011132118.1. NC_005072.1.

Genome annotation databases

EnsemblBacteriaiCAE18942; CAE18942; PMM0483.
GeneIDi1726761.
KEGGipmm:PMM0483.
PATRICi23031736. VBIProMar68066_0538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548174 Genomic DNA. Translation: CAE18942.1.
RefSeqiNP_892601.1. NC_005072.1.
WP_011132118.1. NC_005072.1.

3D structure databases

ProteinModelPortaliQ7V2J3.
SMRiQ7V2J3. Positions 5-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi59919.PMM0483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE18942; CAE18942; PMM0483.
GeneIDi1726761.
KEGGipmm:PMM0483.
PATRICi23031736. VBIProMar68066_0538.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciPMAR59919:GJMQ-503-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCMP1986 / MED4.

Entry informationi

Entry nameiGSA_PROMP
AccessioniPrimary (citable) accession number: Q7V2J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2003
Last modified: January 7, 2015
This is version 84 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.