GSA_THET8
ID GSA_THET8 Reviewed; 424 AA.
AC Q5SJS4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA {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 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375}; OrderedLocusNames=TTHA0934;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; AP008226; BAD70757.1; -; Genomic_DNA.
DR RefSeq; WP_011228305.1; NC_006461.1.
DR RefSeq; YP_144200.1; NC_006461.1.
DR PDB; 2E7U; X-ray; 1.90 A; A=1-424.
DR PDBsum; 2E7U; -.
DR AlphaFoldDB; Q5SJS4; -.
DR SMR; Q5SJS4; -.
DR STRING; 300852.55772316; -.
DR EnsemblBacteria; BAD70757; BAD70757; BAD70757.
DR GeneID; 3168378; -.
DR KEGG; ttj:TTHA0934; -.
DR PATRIC; fig|300852.9.peg.917; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_0; -.
DR OMA; WGPLIFG; -.
DR PhylomeDB; Q5SJS4; -.
DR UniPathway; UPA00251; UER00317.
DR EvolutionaryTrace; Q5SJS4; -.
DR Proteomes; UP000000532; 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..424
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243636"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2E7U"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2E7U"
FT TURN 240..245
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2E7U"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 321..343
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:2E7U"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:2E7U"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2E7U"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:2E7U"
SQ SEQUENCE 424 AA; 46034 MW; 8134C11065EEFF77 CRC64;
MERPISEAYF QEAKRHIPGG VSSPVRAFKA VGGTPPFLVR GEGAYVWDAD GNRYLDYVMS
WGPLILGHAH PKVLARVRET LERGLTFGAP SPLEVALAKK VKRAYPFVDL VRFVNSGTEA
TMSALRLARG YTGRPYIVKF RGNYHGHADG LLVEAGSGAL TLGVPSSAGV PEEYAKLTLV
LEYNDPEGLR EVLKRRGEEI AAIIFEPVVG NAGVLVPTED FLKALHEAKA YGVLLIADEV
MTGFRLAFGG ATELLGLKPD LVTLGKILGG GLPAAAYAGR REIMEKVAPL GPVYQAGTLS
GNPLAMAAGL ATLELLEENP GYYAYLEDLG ARLEAGLKEV LKEKGLPHTV NRVGSMITVF
FTEGPVVTFQ DARRTDTELF KRFFHGLLDR GIYWPPSNFE AAFLSVAHRE EDVEKTLEAL
RKAL
