ID   GSA_BACSU               Reviewed;         430 AA.
AC   P30949;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 156.
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; Synonyms=hemK; OrderedLocusNames=BSU28120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1672867; DOI=10.1128/jb.173.8.2590-2599.1991;
RA   Hansson M., Rutberg L., Schroeder I., Hederstedt L.;
RT   "The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the
RT   biosynthetic pathway from glutamate to uroporphyrinogen III.";
RL   J. Bacteriol. 173:2590-2599(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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}.
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DR   EMBL; M57676; AAA22515.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14772.1; -; Genomic_DNA.
DR   PIR; D42728; D42728.
DR   RefSeq; NP_390690.1; NC_000964.3.
DR   RefSeq; WP_004398699.1; NZ_JNCM01000036.1.
DR   PDB; 3BS8; X-ray; 2.30 A; A=1-430.
DR   PDBsum; 3BS8; -.
DR   AlphaFoldDB; P30949; -.
DR   SMR; P30949; -.
DR   STRING; 224308.BSU28120; -.
DR   jPOST; P30949; -.
DR   PaxDb; 224308-BSU28120; -.
DR   EnsemblBacteria; CAB14772; CAB14772; BSU_28120.
DR   GeneID; 937490; -.
DR   KEGG; bsu:BSU28120; -.
DR   PATRIC; fig|224308.179.peg.3055; -.
DR   eggNOG; COG0001; Bacteria.
DR   InParanoid; P30949; -.
DR   OrthoDB; 9807885at2; -.
DR   PhylomeDB; P30949; -.
DR   BioCyc; BSUB:BSU28120-MONOMER; -.
DR   BRENDA; 5.4.3.8; 658.
DR   UniPathway; UPA00251; UER00317.
DR   EvolutionaryTrace; P30949; -.
DR   Proteomes; UP000001570; 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..430
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120393"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   TURN            30..33
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           93..105
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           118..133
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           187..197
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           222..233
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   TURN            242..247
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           252..256
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           268..271
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           283..286
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           305..316
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           320..343
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          356..364
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           369..372
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           377..389
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   STRAND          396..400
FT                   /evidence="ECO:0007829|PDB:3BS8"
FT   HELIX           410..429
FT                   /evidence="ECO:0007829|PDB:3BS8"
SQ   SEQUENCE   430 AA;  46449 MW;  FBC7CF1784C46017 CRC64;
     MRSYEKSKTA FKEAQKLMPG GVNSPVRAFK SVDMDPIFME RGKGSKIFDI DGNEYIDYVL
     SWGPLILGHT NDRVVESLKK VAEYGTSFGA PTEVENELAK LVIDRVPSVE IVRMVSSGTE
     ATMSALRLAR GYTGRNKILK FEGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGIAKNTI
     TVPYNDLESV KLAFQQFGED IAGVIVEPVA GNMGVVPPQE GFLQGLRDIT EQYGSLLIFD
     EVMTGFRVDY NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEQIA PSGPIYQAGT
     LSGNPLAMTA GLETLKQLTP ESYKNFIKKG DRLEEGISKT AGAHGIPHTF NRAGSMIGFF
     FTNEPVINYE TAKSSDLKLF ASYYKGMANE GVFLPPSQFE GLFLSTAHTD EDIENTIQAA
     EKVFAEISRR
//