ID GSA_VIBCM Reviewed; 432 AA. AC C3LSN1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 74. 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=VCM66_0584; OS Vibrio cholerae serotype O1 (strain M66-2). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=579112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M66-2; RX PubMed=19115014; DOI=10.1371/journal.pone.0004053; RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., RA Wang W., Wang J., Qian W., Li D., Wang L.; RT "A recalibrated molecular clock and independent origins for the cholera RT pandemic clones."; RL PLoS ONE 3:E4053-E4053(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; CP001233; ACP04907.1; -; Genomic_DNA. DR RefSeq; WP_000167257.1; NC_012578.1. DR AlphaFoldDB; C3LSN1; -. DR SMR; C3LSN1; -. DR GeneID; 69720620; -. DR KEGG; vcm:VCM66_0584; -. DR HOGENOM; CLU_016922_1_5_6; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000001217; Chromosome I. 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..432 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_1000201038" FT MOD_RES 265 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375" SQ SEQUENCE 432 AA; 46182 MW; 963BD21BE460C714 CRC64; MTKSAELYQK AQTTIPGGVN SPVRAFNGVG GSPIFIDRAD GALIFDADGK AYIDYVGSWG PMILGHNHAV IREAVIQAAQ RGLSFGAPTE MEITMAELVS ELVPSMEQLR MVNSGTEATM SAIRLARGYT GRDKIIKFEG CYHGHADSLL VKAGSGALTL GQPSSPGVPA DFAKHTLTAR FNDLDSVREL FAANQGEIAC IIVEPVAGNM NCIPPVEGFH EGLREICDQE GALLIFDEVM TGFRVALGGA QAHYNIKPDL TTLGKVIGGG MPVGAFGGRR EVMQYIAPTG PVYQAGTLSG NPIAMAAGYA CLNLLREEGN EKRLAAKTKQ LADGFKSLAD QHGIPLLVHQ VGGMFGFFFT EQETVTCYED VARCDVERFK RFFHLMLQHG VYLAPSAFEA SFTSLAHGSK EIEATLEAAD RSFAILAAEA KA //