GSA1_BACAN
ID GSA1_BACAN Reviewed; 434 AA.
AC Q81YV0; Q6I3Q1; Q6KXG4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT 1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN OrderedLocusNames=BA_0531, GBAA_0531, BAS0499;
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; AAP24552.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52830.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29625.1; -; Genomic_DNA.
DR RefSeq; NP_843066.1; NC_003997.3.
DR RefSeq; WP_000260527.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_026779.1; NC_005945.1.
DR PDB; 3L44; X-ray; 2.05 A; A/B=1-434.
DR PDBsum; 3L44; -.
DR AlphaFoldDB; Q81YV0; -.
DR SMR; Q81YV0; -.
DR IntAct; Q81YV0; 4.
DR STRING; 261594.GBAA_0531; -.
DR DNASU; 1087796; -.
DR EnsemblBacteria; AAP24552; AAP24552; BA_0531.
DR EnsemblBacteria; AAT29625; AAT29625; GBAA_0531.
DR GeneID; 45020579; -.
DR KEGG; ban:BA_0531; -.
DR KEGG; bar:GBAA_0531; -.
DR KEGG; bat:BAS0499; -.
DR PATRIC; fig|198094.11.peg.530; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OMA; NFGMVEP; -.
DR UniPathway; UPA00251; UER00317.
DR EvolutionaryTrace; Q81YV0; -.
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..434
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT /id="PRO_0000243536"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3L44"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3L44"
FT TURN 244..249
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3L44"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3L44"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3L44"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 307..320
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 325..346
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3L44"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:3L44"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:3L44"
SQ SEQUENCE 434 AA; 46432 MW; 3C6A06070A078FEC CRC64;
MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPIA MERGKGAYFW DVDGNKYIDY
LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF AKMLKEAMPA LDKVRFVNSG
TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE
VITVPFNNVE TLKEALDKWG HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI
YDEVITAFRF MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA
GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAAKHNID ITLNRLKGAL
TVYFTTNTIE DYDAAQDTDG EMFGKFFKLM LQEGVNLAPS KYEAWFLTTE HTKEDIEYTI
EAVGRAFAAL ADNK
