ID GSA_AERPE Reviewed; 429 AA. AC Q9Y9I9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 27-MAR-2024, entry version 134. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase; DE Short=GSA; DE EC=5.4.3.8; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase; DE Short=GSA-AT; GN Name=hemL; OrderedLocusNames=APE_2299.1; OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / OS K1). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=10382966; DOI=10.1093/dnares/6.2.83; RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.; RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, RT Aeropyrum pernix K1."; RL DNA Res. 6:83-101(1999). 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; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {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; BA000002; BAA81311.2; -; Genomic_DNA. DR PIR; G72456; G72456. DR PDB; 2EPJ; X-ray; 1.70 A; A=2-429. DR PDB; 2ZSL; X-ray; 1.70 A; A=2-429. DR PDB; 2ZSM; X-ray; 2.30 A; A/B/C=2-429. DR PDBsum; 2EPJ; -. DR PDBsum; 2ZSL; -. DR PDBsum; 2ZSM; -. DR AlphaFoldDB; Q9Y9I9; -. DR SMR; Q9Y9I9; -. DR STRING; 272557.APE_2299.1; -. DR EnsemblBacteria; BAA81311; BAA81311; APE_2299.1. DR KEGG; ape:APE_2299.1; -. DR PATRIC; fig|272557.25.peg.1533; -. DR eggNOG; arCOG00918; Archaea. DR UniPathway; UPA00251; UER00317. DR EvolutionaryTrace; Q9Y9I9; -. DR Proteomes; UP000002518; 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: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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isomerase; Porphyrin biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..429 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_0000120476" FT MOD_RES 266 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" FT HELIX 5..14 FT /evidence="ECO:0007829|PDB:2EPJ" FT TURN 15..17 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 25..29 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 91..104 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 116..131 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 185..195 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 218..231 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:2EPJ" FT TURN 240..245 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 250..255 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:2EPJ" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:2EPJ" FT TURN 298..301 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 303..318 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 321..343 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:2EPJ" FT STRAND 355..360 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 368..371 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 376..388 FT /evidence="ECO:0007829|PDB:2EPJ" FT HELIX 409..427 FT /evidence="ECO:0007829|PDB:2EPJ" SQ SEQUENCE 429 AA; 45954 MW; 6CC7C5A97EE1F65C CRC64; MASGEKSRML FERTKELFPG GVNSPVRAAV KPYPFYVKRG EGAYLYTVDG ARIVDLVLAY GPLILGHKHP RVLEAVEEAL ARGWLYGAPG EAEVLLAEKI LGYVKRGGMI RFVNSGTEAT MTAIRLARGY TGRDLILKFD GCYHGSHDAV LVAAGSAAAH YGVPTSAGVP EAVARLTLVT PYNDVEALER VFAEYGDRIA GVIVEPVIAN AGVIPPRREF LAALQRLSRE SGALLILDEV VTGFRLGLEG AQGYFNIEGD IIVLGKIIGG GFPVGAVAGS REVMSLLTPQ GKVFNAGTFN AHPITMAAGL ATLKALEEEP VYSVSREAAK ALEEAASEVL DRTGLPYTIN RVESMMQLFI GVEEVSNAAQ ARKADKKFYV KLHEEMLRRG VFIAPSNLEA VFTGLPHQGE ALEIAVEGLR SSLKTVLGS //