ID GSA_PSEAE Reviewed; 427 AA. AC P48247; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 154. 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=PA3977; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=7565600; DOI=10.1007/bf02191605; RA Hungerer C., Troup B., Romling U., Jahn D.; RT "Cloning, mapping and characterization of the Pseudomonas aeruginosa hemL RT gene."; RL Mol. Gen. Genet. 248:375-380(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. 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; X82072; CAA57575.1; -; Genomic_DNA. DR EMBL; AE004091; AAG07364.1; -; Genomic_DNA. DR PIR; G83149; G83149. DR PIR; S57898; S57898. DR RefSeq; NP_252666.1; NC_002516.2. DR RefSeq; WP_003093150.1; NZ_QZGE01000001.1. DR PDB; 5I92; X-ray; 1.75 A; A/B/C/D/E/F=1-427. DR PDBsum; 5I92; -. DR AlphaFoldDB; P48247; -. DR SMR; P48247; -. DR STRING; 208964.PA3977; -. DR PaxDb; 208964-PA3977; -. DR GeneID; 880859; -. DR KEGG; pae:PA3977; -. DR PATRIC; fig|208964.12.peg.4169; -. DR PseudoCAP; PA3977; -. DR HOGENOM; CLU_016922_1_5_6; -. DR InParanoid; P48247; -. DR OrthoDB; 9801052at2; -. DR PhylomeDB; P48247; -. DR BioCyc; PAER208964:G1FZ6-4051-MONOMER; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000002438; 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..427 FT /note="Glutamate-1-semialdehyde 2,1-aminomutase" FT /id="PRO_0000120433" FT MOD_RES 265 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" FT CONFLICT 157 FT /note="A -> S (in Ref. 1; CAA57575)" FT /evidence="ECO:0000305" FT HELIX 3..11 FT /evidence="ECO:0007829|PDB:5I92" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 22..25 FT /evidence="ECO:0007829|PDB:5I92" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 69..79 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 90..102 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 115..130 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 219..230 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:5I92" FT TURN 239..244 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 249..254 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:5I92" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 302..314 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 320..341 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 347..351 FT /evidence="ECO:0007829|PDB:5I92" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 368..373 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 376..388 FT /evidence="ECO:0007829|PDB:5I92" FT HELIX 409..424 FT /evidence="ECO:0007829|PDB:5I92" SQ SEQUENCE 427 AA; 45398 MW; 670EB87D144E2D28 CRC64; MSRSETLFNN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVLDEDDK RYVDYVGSWG PMILGHSHPD VLDAVRRQLD HGLSYGAPTA LEVEMADLVC SMVPSMEMVR MVSSGTEATM SAIRLARGYT GRDSIIKFEG CYHGHSDSLL VKAGSGALTF GVPNSPGVPA AFAKHTLTLP FNDIEAVRKT LGEVGKEVAC IIVEPVAGNM NCVPPAPGFL EGLREACDEH GVVLIFDEVM TGFRVALGGA QAYYGVTPDL STFGKIIGGG MPVGAFGGKR EIMQQISPLG PVYQAGTLSG NPLAMAAGLT TLRLISRPGF HDELTAYTTR MLDGLQQRAD AAGIPFVTTQ AGGMFGLYFS GADAIVTFED VMASDVERFK RFFHLMLDGG VYLAPSAFEA GFTSIAHGDK ELEITLNAAE KAFAALK //