GSA_BACSU
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 03-AUG-2022, entry version 149.
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; Firmicutes; 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; P30949; -.
DR PRIDE; P30949; -.
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 OMA; WGPLIFG; -.
DR PhylomeDB; P30949; -.
DR BioCyc; BSUB:BSU28120-MON; -.
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; 3.40.640.10; -; 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..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
