ID GSA_SYNS9 Reviewed; 428 AA. AC Q3AWP4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 27-MAR-2024, entry version 113. 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=Syncc9902_1701; OS Synechococcus sp. (strain CC9902). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=316279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9902; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Synechococcus sp. CC9902."; RL Submitted (AUG-2005) 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: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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis. {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 -!- SEQUENCE CAUTION: CC Sequence=ABB26659.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000097; ABB26659.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; Q3AWP4; -. DR SMR; Q3AWP4; -. DR STRING; 316279.Syncc9902_1701; -. DR KEGG; sye:Syncc9902_1701; -. DR eggNOG; COG0001; Bacteria. DR HOGENOM; CLU_016922_1_5_3; -. DR UniPathway; UPA00251; UER00317. DR UniPathway; UPA00668; -. DR Proteomes; UP000002712; Chromosome. 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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule. 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 Chlorophyll biosynthesis; Cytoplasm; Isomerase; Porphyrin biosynthesis; KW Pyridoxal phosphate. FT CHAIN 1..428 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_0000243628" FT MOD_RES 267 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375" SQ SEQUENCE 428 AA; 44935 MW; FC11BD86952A8B27 CRC64; MNTSRSQAIF GAAQGLMPGG VSSPVRAFKS VGGQPIVFDR VKGPYAWDVD GNKYIDYIGS WGPAICGHAH PEVISALQEA IEKGTSFGAP CALENTLAEM VIDAVPSVEM VRFVNSGTEA CMAVLRLMRA FTGRDKVIKF EGCYHGHADM FLVKAGSGVA TLGLPDSPGV PRSTTANTLT APYNDLEAVK ALFAENPDAI SGVILEPIVG NAGFIQPEPG FLEGLRELTK ENGALLVFDE VMTGFRISYG GAQAHFGVTP DLTTMGKVIG GGLPVGAYGG RADIMQMVSP AGPMYQAGTL SGNPLAMTAG IKTLELLKQP GTYEKLAATT ERLISGIKTA AGEAGFPITG GSVSAMFGFF LCEGPVRNFE EAKATDSERF GRLHRAMLER GVYLAPSAYE AGFTSLAHSD ADIEATINAF RESFAVIG //