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Q9JXW0

- GSA_NEIMB

UniProt

Q9JXW0 - GSA_NEIMB

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Neisseria meningitidis serogroup B (strain MC58)
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 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. 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

BioCyciNMEN122586:GHGG-1920-MONOMER.
UniPathwayiUPA00251; UER00317.

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:NMB1864
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000425: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ9JXW0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi122586.NMB1864.

Structurei

3D structure databases

ProteinModelPortaliQ9JXW0.
SMRiQ9JXW0. Positions 3-420.
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.
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.

Q9JXW0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNRNEILFDR AKAIIPGGVN SPVRAFGSVG GVPRFIKKAE GAYVWDENGT
60 70 80 90 100
RYTDYVGSWG PAIVGHAHPE VVETVCEAAL GGLSFGAPTE GEIVIAEEIA
110 120 130 140 150
KIMPSVERLR LVSSGTEATM TAIRLARGFT GRDKIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGLLTF GNPSSAGVPA DFTKHTLVLE YNNIAQLEEA FAQSGNEIAC
210 220 230 240 250
VIVEPFVGNM NLVRPTEAFV KALRGLTEKY GAVLIYDEVM TGFRVALGGA
260 270 280 290 300
QSLHGITPDL TTMGKVIGGG MPLAAFGGRK DIMECISPLG GVYQAGTLSG
310 320 330 340 350
NPIAVAAGLK TLEIIQREGF YENLTARTEQ LVQGFRTAAD AAGIEFTADS
360 370 380 390 400
VGGMFGLYFA AHAPRNYADM ARSNIEGFKQ FFHGMLDRNV AFGPSAYEAG
410 420
FVSAAHTPEL IDETVAVAVE VFKAMAE
Length:427
Mass (Da):45,315
Last modified:October 1, 2000 - v1
Checksum:i2ECC6C2E76A1B558
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF42198.1.
PIRiA81034.
RefSeqiNP_274860.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF42198; AAF42198; NMB1864.
GeneIDi904324.
KEGGinme:NMB1864.
PATRICi20359755. VBINeiMen85645_2383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF42198.1 .
PIRi A81034.
RefSeqi NP_274860.1. NC_003112.2.

3D structure databases

ProteinModelPortali Q9JXW0.
SMRi Q9JXW0. Positions 3-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122586.NMB1864.

Proteomic databases

PRIDEi Q9JXW0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF42198 ; AAF42198 ; NMB1864 .
GeneIDi 904324.
KEGGi nme:NMB1864.
PATRICi 20359755. VBINeiMen85645_2383.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci NMEN122586:GHGG-1920-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: MC58.

Entry informationi

Entry nameiGSA_NEIMB
AccessioniPrimary (citable) accession number: Q9JXW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 102 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