ID A0A2D7NQV5_9DELT Unreviewed; 427 AA. AC A0A2D7NQV5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, entry version 2. 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}; RN [1] {ECO:0000313|EMBL:MAJ49303.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED631 {ECO:0000313|EMBL:MAJ49303.1}; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from RT the Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5- CC aminolevulinate. {ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS00768761}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS00768749}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 2/2. {ECO:0000256|SAAS:SAAS00768757}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS00768743}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00375, ECO:0000256|SAAS:SAAS00768745}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. 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 ECO:0000256|SAAS:SAAS00768755}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|SAAS:SAAS00768759}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|SAAS:SAAS00768753}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00768738}. FT MOD_RES 267 267 N6-(pyridoxal phosphate)lysine. FT {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 //