ID GSA_SHEAM Reviewed; 427 AA. AC A1S3U0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 01-SEP-2009, entry version 19. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase; DE Short=GSA; DE EC=5.4.3.8; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase; DE Short=GSA-AT; GN Name=hemL; OrderedLocusNames=Sama_0839; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Fredrickson J., Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5- CC aminolevulinate. CC -!- COFACTOR: Pyridoxal phosphate. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000507; ABL99046.1; -; Genomic_DNA. DR RefSeq; YP_926716.1; -. DR STRING; A1S3U0; -. DR GeneID; 4603091; -. DR GenomeReviews; CP000507_GR; Sama_0839. DR KEGG; saz:Sama_0839; -. DR NMPDR; fig|326297.7.peg.790; -. DR OMA; A1S3U0; NCVPPAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase ac...; IEA:HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00375; -; 1. DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR11986; Aminotrans_3; 1. DR Pfam; PF00202; Aminotran_3; 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 1 427 Glutamate-1-semialdehyde 2,1-aminomutase. FT /FTId=PRO_0000300944. FT MOD_RES 265 265 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 427 AA; 45922 MW; 39F8F15C3CCF2392 CRC64; MTRSETLFEQ AKKTIPGGVN SPVRAFNGVG GTPRFIEKAD GAYIYDADGK AYIDYVGSWG PMILGHNHPS IREAVLKAVH NGLSFGAPTE LEVIMAEKVI EMVPSMDQVR MVSSGTEATM SAIRLARGYT KRDKILKFEG CYHGHADCLL VKAGSGALTL GQPSSPGIPE DFAKHTLTAV YNDLESVQSF FDQYPEDIAC IIIEPVAGNM NCIPPVPGFL EGLRALCDKY GALFIIDEVM TGFRVSRSGA QGHYGVTPDL TTLGKVIGGG MPVGAFGGKK DVMQYLAPAG PVYQAGTLSG NPIAMTAGLA QLDALCADGL YEELAAKTKR IAEGFKAAAD KHGIPMAINY VGGMFGFFFT DEQHITRFDQ VTRCNMDHFR AFYHGMLDEG VYLAPSAYEA GFLSMAHGDK EIEETLAAAD RVLARMK //