GSA2_BACAN
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 25-MAY-2022, entry version 134.
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; Firmicutes; 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; 260799.BAS4358; -.
DR DNASU; 1083709; -.
DR EnsemblBacteria; AAP28392; AAP28392; BA_4693.
DR EnsemblBacteria; AAT33816; AAT33816; GBAA_4693.
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 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; 3.40.640.10; -; 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 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
