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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processPorphyrin biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 1UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
Short name:
GSA-AT 1UniRule annotation
Gene namesi
Name:hemL1UniRule annotation
Ordered Locus Names:BA_0531, GBAA_0531, BAS0499
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000000427 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002435361 – 434Glutamate-1-semialdehyde 2,1-aminomutase 1Add BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei270N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ81YV0, 4 interactors
STRINGi260799.BAS0499

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 18Combined sources13
Helixi20 – 22Combined sources3
Helixi26 – 28Combined sources3
Helixi31 – 33Combined sources3
Beta strandi41 – 46Combined sources6
Beta strandi48 – 51Combined sources4
Beta strandi56 – 59Combined sources4
Helixi62 – 64Combined sources3
Helixi74 – 86Combined sources13
Helixi95 – 107Combined sources13
Beta strandi112 – 119Combined sources8
Helixi120 – 135Combined sources16
Beta strandi139 – 143Combined sources5
Helixi152 – 155Combined sources4
Beta strandi167 – 170Combined sources4
Helixi175 – 178Combined sources4
Beta strandi181 – 184Combined sources4
Helixi189 – 199Combined sources11
Helixi200 – 202Combined sources3
Beta strandi203 – 208Combined sources6
Beta strandi210 – 212Combined sources3
Helixi224 – 233Combined sources10
Turni234 – 236Combined sources3
Beta strandi238 – 242Combined sources5
Turni244 – 249Combined sources6
Beta strandi250 – 253Combined sources4
Helixi255 – 259Combined sources5
Beta strandi264 – 268Combined sources5
Turni272 – 275Combined sources4
Beta strandi279 – 283Combined sources5
Helixi285 – 288Combined sources4
Turni292 – 294Combined sources3
Beta strandi295 – 297Combined sources3
Turni302 – 305Combined sources4
Helixi307 – 320Combined sources14
Helixi325 – 346Combined sources22
Beta strandi351 – 356Combined sources6
Beta strandi359 – 367Combined sources9
Helixi372 – 377Combined sources6
Helixi380 – 392Combined sources13
Helixi413 – 432Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L44X-ray2.05A/B1-434[»]
ProteinModelPortaliQ81YV0
SMRiQ81YV0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81YV0

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001 LUCA
HOGENOMiHOG000020210
KOiK01845
OMAiHEVTFAK

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00375 HemL_aminotrans_3, 1 hit
InterProiView protein in InterPro
IPR004639 4pyrrol_synth_GluAld_NH2Trfase
IPR005814 Aminotrans_3
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00713 hemL, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q81YV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPIA MERGKGAYFW
60 70 80 90 100
DVDGNKYIDY LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF
110 120 130 140 150
AKMLKEAMPA LDKVRFVNSG TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH
160 170 180 190 200
SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE VITVPFNNVE TLKEALDKWG
210 220 230 240 250
HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI YDEVITAFRF
260 270 280 290 300
MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA
310 320 330 340 350
GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAAKHNID
360 370 380 390 400
ITLNRLKGAL TVYFTTNTIE DYDAAQDTDG EMFGKFFKLM LQEGVNLAPS
410 420 430
KYEAWFLTTE HTKEDIEYTI EAVGRAFAAL ADNK
Length:434
Mass (Da):46,432
Last modified:June 1, 2003 - v1
Checksum:i3C6A06070A078FEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA Translation: AAP24552.1
AE017225 Genomic DNA Translation: AAT52830.1
AE017334 Genomic DNA Translation: AAT29625.1
RefSeqiNP_843066.1, NC_003997.3
WP_000260527.1, NZ_PPES01000045.1
YP_026779.1, NC_005945.1

Genome annotation databases

EnsemblBacteriaiAAP24552; AAP24552; BA_0531
AAT29625; AAT29625; GBAA_0531
AAT52830; AAT52830; BAS0499
GeneIDi1087796
2852947
KEGGiban:BA_0531
bar:GBAA_0531
bat:BAS0499
PATRICifig|198094.11.peg.530

Similar proteinsi

Entry informationi

Entry nameiGSA1_BACAN
AccessioniPrimary (citable) accession number: Q81YV0
Secondary accession number(s): Q6I3Q1, Q6KXG4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: May 23, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health