GSA_STRMK
ID GSA_STRMK Reviewed; 429 AA.
AC B2FT35;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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}; OrderedLocusNames=Smlt3873;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(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; AM743169; CAQ47277.1; -; Genomic_DNA.
DR RefSeq; WP_012481173.1; NC_010943.1.
DR PDB; 6W80; X-ray; 1.40 A; A=1-429.
DR PDBsum; 6W80; -.
DR AlphaFoldDB; B2FT35; -.
DR SMR; B2FT35; -.
DR STRING; 522373.Smlt3873; -.
DR EnsemblBacteria; CAQ47277; CAQ47277; Smlt3873.
DR KEGG; sml:Smlt3873; -.
DR PATRIC; fig|522373.3.peg.3648; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000008840; 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; 3.40.640.10; -; 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 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_1000121926"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6W80"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6W80"
FT TURN 241..246
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6W80"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6W80"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 322..344
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6W80"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 377..389
FT /evidence="ECO:0007829|PDB:6W80"
FT HELIX 410..427
FT /evidence="ECO:0007829|PDB:6W80"
SQ SEQUENCE 429 AA; 45067 MW; 62C75E93A51E934A CRC64;
MNHDQSHALF SRAQQLLPGG VNSPVRAFKS VGGEPFFVER ADGAYLYDVD GNRYIDYVGS
WGPMIVGHNH PAVRQAVKKA IDNGLSFGAP CAGEVTMAET ITRLVPSCEM VRMVNSGTEA
TLSAIRLARG ATGRNRIVKF EGCYHGHGDS FLVKAGSGML TLGVPTSPGV PAGLSELTLT
LPYNDFEAAT ALFEQQGDDI AGLIIEPVVG NANCIPPREG YLQHLRALCT KHGALLIFDE
VMTGFRVALG GAQAHYGITP DLTTFGKIIG GGMPVGAYGG RRELMQQIAP AGPIYQAGTL
SGNPVAMAAG LAMLELVQQP GFHADLAERT ARLCAGLEAA AADAGVAVTT TRVGAMFGLF
FTSEKVETYA QATACDIPAF NRFFHAMLEQ GVFLAPSAYE AGFLSSAHDD AVIEATLAAA
RVAFRAAKG
