ID A0A857M415_9ACTN Unreviewed; 447 AA. AC A0A857M415; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 22-FEB-2023, entry version 6. 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 pseudamarae. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=2831662 {ECO:0000313|EMBL:QHN36582.1}; RN [1] {ECO:0000313|EMBL:QHN36582.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CON9 {ECO:0000313|EMBL:QHN36582.1}; RX PubMed=33927381; RA Batinovic S., Rose J.J.A., Ratcliffe J., Seviour R.J., Petrovski S.; RT "Cocultivation of an ultrasmall environmental parasitic bacterium with RT lytic ability against bacteria associated with wastewater foams."; RL Nat. Microbiol. 6:703-711(2021). 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 AlphaFoldDB; A0A857M415; -. 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1. DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 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 //