ID GSA1_BACC0 Reviewed; 434 AA.
AC B7JNG6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1;
DE Short=GSA 1;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase 1;
DE Short=GSA-AT 1;
GN Name=hemL1; OrderedLocusNames=BCAH820_0514;
OS Bacillus cereus (strain AH820).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC aminolevulinate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
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DR EMBL; CP001283; ACK91919.1; -; Genomic_DNA.
DR RefSeq; YP_002449506.1; NC_011773.1.
DR ProteinModelPortal; B7JNG6; -.
DR STRING; 405535.BCAH820_0514; -.
DR EnsemblBacteria; ACK91919; ACK91919; BCAH820_0514.
DR GeneID; 7192187; -.
DR KEGG; bcu:BCAH820_0514; -.
DR PATRIC; 18837858; VBIBacCer122868_0486.
DR eggNOG; COG0001; -.
DR HOGENOM; HOG000020210; -.
DR KO; K01845; -.
DR OMA; KVENYEQ; -.
DR ProtClustDB; PRK12389; -.
DR BioCyc; BCER405535:GHSL-5092-MONOMER; -.
DR UniPathway; UPA00251; UER00317.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:HAMAP.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1; -.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR PANTHER; PTHR11986:SF5; PTHR11986:SF5; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW Pyridoxal phosphate.
FT CHAIN 1 434 Glutamate-1-semialdehyde 2,1-aminomutase
FT 1.
FT /FTId=PRO_0000382267.
FT MOD_RES 270 270 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 434 AA; 46418 MW; 3C6CDBB1D7B78FEC CRC64;
MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPIA MERGKGAYFW DVDGNKYIDY
LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF AKMLKEAMPA LDKVRFVNSG
TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE
VITVPFNNVE TLKEALDKWG HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI
YDEVITAFRF MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA
GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAAKHNID ITLNRLKGAL
TVYFTTNTIE DYDAAQDTDG EMFGNFFKLM LQEGVNLAPS KYEAWFLTTE HTKEDIEYTI
EAVGRAFAAL ADNK
//
