ID A0A2D7NQV5_9DELT Unreviewed; 427 AA. AC A0A2D7NQV5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-JUN-2021, entry version 11. 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:MAJ49303.1}; GN ORFNames=CL937_06310 {ECO:0000313|EMBL:MAJ49303.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ49303.1, ECO:0000313|Proteomes:UP000226880}; RN [1] {ECO:0000313|Proteomes:UP000226880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) 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|ARBA:ARBA00001579, CC 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. CC {ECO:0000256|ARBA:ARBA00023444}. 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. {ECO:0000256|RuleBase:RU003560}. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MAJ49303.1}. 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; NZHX01000091; MAJ49303.1; -; Genomic_DNA. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000226880; Unassembled WGS sequence. 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; 3.40.640.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. 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 267 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375" SQ SEQUENCE 427 AA; 45887 MW; 7FA6879E3FD7C50D CRC64; MKISESKKLF SRAQEVMPGG VNSPVRAFKS VQSEPLFITH AKGSRLFDAD GNSFIDYIGS WGPMILGHAD PRITSEIEKA VQKGTSFGTP TEGEIELAEM ISDAVPSVEM VRLVNSGSEA AMGALRVARG FTGRDKIIKF EGCYHGSVDA LLVKAGSGAT TLGIPDSPGV PQSFTEHTLS APFNXLXAVI ELTENFPDEI AAIVLEPVAG NMGMIPPEHG FLQGLRELCD REGILLIFDE VMTGFRVDFS GAQALFQVMP DLSIFGKVIG GGLPVGAYGG RREIMLQVAP AGPVYQAGTL SGNPIAVSAG KTMLKILKEE DPYADLGRKT ATLNEALSDA AKKKGIPLET CSMGGMFGFF FSEKKVRNYE DALKCNRDYF ITFFREVLSR GIYLAPSPFE SLFLSSSHSE ADLDQTIEAF QHGLAAI //