ID GSA_ECODH Reviewed; 426 AA. AC B1XD24; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 16-JUN-2009, entry version 13. 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=ECDH10B_0134; OS Escherichia coli (strain DH10B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18245285; DOI=10.1128/JB.01695-07; RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., RA Posfai G., Weinstock G.M., Blattner F.R.; RT "The complete genome sequence of Escherichia coli DH10B: insights into RT the biology of a laboratory workhorse."; RL J. Bacteriol. 190:2597-2606(2008). 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; CP000948; ACB01333.1; -; Genomic_DNA. DR RefSeq; YP_001729111.1; -. DR GeneID; 6062269; -. DR GenomeReviews; CP000948_GR; ECDH10B_0134. DR KEGG; ecd:ECDH10B_0134; -. DR OMA; B1XD24; 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 1 426 Glutamate-1-semialdehyde 2,1-aminomutase. FT /FTId=PRO_1000121883. FT MOD_RES 265 265 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 426 AA; 45366 MW; BED817E100468CF2 CRC64; MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT ELVPTMDMVR MVNSGTEATM SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFAKYTLTCT YNDLASVRAA FEQYPQEIAC IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH VGGMFGIFFT DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA GFMSVAHSME DINNTIDAAR RVFAKL //