ID A0A857M415_9ACTN Unreviewed; 447 AA. AC A0A857M415; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375}; DE Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375}; DE EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375}; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375}; DE Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375}; GN Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375, GN ECO:0000313|EMBL:QHN36582.1}; GN ORFNames=GII31_18465 {ECO:0000313|EMBL:QHN36582.1}; OS Gordonia amarae. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=36821 {ECO:0000313|EMBL:QHN36582.1}; RN [1] {ECO:0000313|EMBL:QHN36582.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 43602 {ECO:0000313|EMBL:QHN36582.1}; RA Batinovic S., Petrovski S.; RT "Whole genome sequencing of Gordonia amarae strains."; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00375}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|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:0000256|ARBA:ARBA00004819}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. CC {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-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; CP045809; QHN36582.1; -; Genomic_DNA. DR UniPathway; UPA00251; UER00317. DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro. 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 {ECO:0000256|HAMAP-Rule:MF_00375}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP- KW Rule:MF_00375}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_00375}. FT MOD_RES 277 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375" SQ SEQUENCE 447 AA; 45278 MW; 49C9AF1B6EC11824 CRC64; MTRPAASGNS PSDANSAALF ERAAQAIPGG VNSPVRAFSA VGGTPRFITS AQGCTLTDAD GNNYVDLVAS WGPMILGHAH PAVVDAVRRA AGTGLSFGAP TEAEIELAEE LIARVDPVEQ VRLVNSGTEA TMSAIRLARG VTGRGKIIKF SGCYHGHVDA LLADAGSGIA TLGLPTSPGV TGASAHDTVV LPYNDLAAVA AAFERYDGQI AAVITEAAAG NMGAVAPVDG FNAGLRELTL RHGALLIVDE VMTGFRVSPA GWYGLEGVAG DLYTFGKVMS GGLPAAAFGG RREIMGHLAP SGPVYQAGTL SGNPVAVAAG LATLRNADAA VYEALDANAD RLASLLTESL SAAGVAHRVQ KAGNLLSVFF TSAAGPVTDY ETVKATETFR FAPFFHALLD GGVYAPPSAF EAWFVSAALD DDAFTTIATA LPAAAAAAAA AIDPRGN //