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 03-AUG-2022, entry version 83. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375}; DE Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375}; DE EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375}; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375}; DE Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375}; GN Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375}; GN OrderedLocusNames=ECDH10B_0134; OS Escherichia coli (strain K12 / DH10B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / DH10B; 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 the RT biology of a laboratory workhorse."; RL J. Bacteriol. 190:2597-2606(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate; CC Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416; CC EC=5.4.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00375}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00375}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00375}. 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; WP_000045315.1; NC_010473.1. DR AlphaFoldDB; B1XD24; -. DR SMR; B1XD24; -. DR PRIDE; B1XD24; -. DR KEGG; ecd:ECDH10B_0134; -. DR HOGENOM; CLU_016922_1_5_6; -. DR OMA; WGPLIFG; -. DR BioCyc; ECOL316385:ECDH10B_RS00680-MON; -. 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:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. 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. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00713; hemL; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate. FT CHAIN 1..426 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_1000121883" FT MOD_RES 265 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375" 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 //