ID GSA_LIMRJ Reviewed; 431 AA. AC B2G9H2; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 27-MAR-2024, entry version 85. 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=LAR_1588; OS Limosilactobacillus reuteri subsp. reuteri (strain JCM 1112) (Lactobacillus OS reuteri). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Limosilactobacillus. OX NCBI_TaxID=557433; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1112; RX PubMed=18487258; DOI=10.1093/dnares/dsn009; RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., RA Hattori M.; RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus RT fermentum reveal a genomic island for reuterin and cobalamin production."; RL DNA Res. 15:151-161(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; AP007281; BAG26104.1; -; Genomic_DNA. DR AlphaFoldDB; B2G9H2; -. DR SMR; B2G9H2; -. DR KEGG; lrf:LAR_1588; -. DR HOGENOM; CLU_016922_1_5_9; -. 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; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00713; hemL; 1. 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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate. FT CHAIN 1..431 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_0000382325" FT MOD_RES 270 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375" SQ SEQUENCE 431 AA; 46682 MW; 8B831E94962EF36C CRC64; MSKLDTTKSK IAFKEAQKYM PGGVNSPVRA FKNVGGDPLF IDHGKDEYIY DIDGNKYIDY VLSWGPLILG HADDHVVAEL DKAVAKGTSY GAPTLQETEL AKIVNKIMPS IEMIRMVSSG TEATMSAIRL ARGYTHRKKI VKFVGNYHGH SDSLLVDAGS GLATFGINTS PGVPDDLAYD TLTVAYNDVA GVKKLFAEHG DEIACAIVEP VAGNMGVIPG TQEFLQTLRN VTNEHGALLI FDEVMSGFRA AYHGVQSLVN ITPDLTTLGK VIGGGLPVGA FGGRREIMEN ITPAGDIYHA GTLSGNPLAM TGGISTLEQL TPDDYVEMDK KVTALTEGIK HAADQYGVPM TVHHVGTMWS YFYNSDPINN FDDVKACDQK LFEKCFWELL AHGVYVAPSQ FETNFISTKH TDEDIEKTIA AFDAAFNAAT K //