GSA2_ANOFW
ID GSA2_ANOFW Reviewed; 431 AA.
AC B7GH35;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 71.
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}; OrderedLocusNames=Aflv_0610;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACJ32991.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000922; ACJ32991.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041638006.1; NC_011567.1.
DR AlphaFoldDB; B7GH35; -.
DR SMR; B7GH35; -.
DR STRING; 491915.Aflv_0610; -.
DR EnsemblBacteria; ACJ32991; ACJ32991; Aflv_0610.
DR KEGG; afl:Aflv_0610; -.
DR PATRIC; fig|491915.6.peg.627; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000000742; 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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..431
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT /id="PRO_0000382251"
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 431 AA; 46825 MW; 6F6DBDBBAAE864F7 CRC64;
MRSYERSKAA YAEAVKLMPG GVNSPVRAFK AVKMDPIFMA RGKGSKIYDI DGNEYIDYVL
SWGPLILGHA NDQVVEALKR VAETGTSFGA PTLIENELAK LVMERMPSIE IIRMVSSGTE
ATMSALRLAR GYTGRNKIVK FEGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPETVAQHTI
TVPYNDLQSV RYAFEKFGED IAAVIVEPVA GNMGVVPPEP GFLQGLRDVT NEYGALLIFD
EVMTGFRVDY YSGQGYYGVT PDLTCLGKVI GGGLPVGAYG GRADIMEKIA PSGPIYQAGT
LSGNPMAMTA GYETLRQLTP ETYEAFKKKA NRLAEGLSEA AKAYHIPHTI NQAGSMIGMF
FTNERVTNYE TAKTSNLDLF ARYYQEMANE GIFLPPSQFE GMFLSTAHTD EDIEKTIEAA
RRAFAKMSDC L