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Q821C1

- GSA_SHIFL

UniProt

Q821C1 - GSA_SHIFL

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Shigella flexneri
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

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:SF0146, S0149
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120440Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiQ821C1.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF0146.

Structurei

3D structure databases

ProteinModelPortaliQ821C1.
SMRiQ821C1. Positions 2-422.
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.

Q821C1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK
60 70 80 90 100
AYIDYVGSWG PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT
110 120 130 140 150
ELVPTMDMVR MVNSGTEATM SAIRLARGFT GRDKIIKFEG CYHGHADCLL
160 170 180 190 200
VKAGSGALTL GQPNSPGVPA DFAKHTLTCT YNDLASVRAA FEQYPQEIAC
210 220 230 240 250
IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA
260 270 280 290 300
QDYFAVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMAAGFA CLNEVAQPGI HETLDELTTR LAEGLLEAAE EAGIPLVVNH
360 370 380 390 400
VGGMFGIFFT DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA
410 420
GFMSVAHSME DINNTIDAAR RVFAKL
Length:426
Mass (Da):45,352
Last modified:June 1, 2003 - v1
Checksum:i6C2C8F07E48ED8D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN41809.1.
AE014073 Genomic DNA. Translation: AAP15690.1.
RefSeqiNP_706102.1. NC_004337.2.
NP_835885.1. NC_004741.1.
WP_000045281.1. NZ_JMRK01000015.1.

Genome annotation databases

EnsemblBacteriaiAAN41809; AAN41809; SF0146.
AAP15690; AAP15690; S0149.
GeneIDi1024471.
1076566.
KEGGisfl:SF0146.
sfx:S0149.
PATRICi18701242. VBIShiFle31049_0163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN41809.1 .
AE014073 Genomic DNA. Translation: AAP15690.1 .
RefSeqi NP_706102.1. NC_004337.2.
NP_835885.1. NC_004741.1.
WP_000045281.1. NZ_JMRK01000015.1.

3D structure databases

ProteinModelPortali Q821C1.
SMRi Q821C1. Positions 2-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF0146.

Proteomic databases

PaxDbi Q821C1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN41809 ; AAN41809 ; SF0146 .
AAP15690 ; AAP15690 ; S0149 .
GeneIDi 1024471.
1076566.
KEGGi sfl:SF0146.
sfx:S0149.
PATRICi 18701242. VBIShiFle31049_0163.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .

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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiGSA_SHIFL
AccessioniPrimary (citable) accession number: Q821C1
Secondary accession number(s): Q7C375
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 85 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