ID   GSA2_BACAN              Reviewed;         429 AA.
AC   Q81LD0; Q6HST3; Q6KM26;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT 2 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL2 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=BA_4693, GBAA_4693, BAS4358;
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
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}.
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DR   EMBL; AE016879; AAP28392.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56656.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33816.1; -; Genomic_DNA.
DR   RefSeq; NP_846906.1; NC_003997.3.
DR   RefSeq; WP_001224513.1; NZ_WXXJ01000027.1.
DR   RefSeq; YP_030605.1; NC_005945.1.
DR   PDB; 3K28; X-ray; 1.95 A; A/B/C/D=1-429.
DR   PDBsum; 3K28; -.
DR   AlphaFoldDB; Q81LD0; -.
DR   SMR; Q81LD0; -.
DR   IntAct; Q81LD0; 22.
DR   STRING; 261594.GBAA_4693; -.
DR   DNASU; 1083709; -.
DR   GeneID; 45024333; -.
DR   KEGG; ban:BA_4693; -.
DR   KEGG; bar:GBAA_4693; -.
DR   KEGG; bat:BAS4358; -.
DR   PATRIC; fig|198094.11.peg.4658; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 9807885at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   EvolutionaryTrace; Q81LD0; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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 2"
FT                   /id="PRO_0000243537"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           93..105
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          110..117
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           118..133
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           187..197
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           222..233
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   TURN            242..247
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           252..257
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           268..271
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           283..286
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   TURN            300..303
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           305..316
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           320..343
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   STRAND          356..364
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           369..372
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           377..389
FT                   /evidence="ECO:0007829|PDB:3K28"
FT   HELIX           410..425
FT                   /evidence="ECO:0007829|PDB:3K28"
SQ   SEQUENCE   429 AA;  46060 MW;  9E56295469536AD0 CRC64;
     MRKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI DGNEYIDYVL
     SWGPLIHGHA NDRVVEALKA VAERGTSFGA PTEIENKLAK LVIERVPSIE IVRMVNSGTE
     ATMSALRLAR GYTGRNKILK FIGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI
     TVAYNDLESV KYAFEQFGDD IACVIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD
     EVMTGFRVAY NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQVA PSGPIYQAGT
     LSGNPLAMAA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHGIPHHI NRAGSMIGIF
     FTDEPVINYD AAKSSNLQFF AAYYREMVEQ GVFLPPSQFE GLFLSTVHSD ADIEATIAAA
     EIAMSKLKA
//