GSA_AERPE
ID GSA_AERPE Reviewed; 429 AA.
AC Q9Y9I9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; OrderedLocusNames=APE_2299.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR EMBL; BA000002; BAA81311.2; -; Genomic_DNA.
DR PIR; G72456; G72456.
DR PDB; 2EPJ; X-ray; 1.70 A; A=2-429.
DR PDB; 2ZSL; X-ray; 1.70 A; A=2-429.
DR PDB; 2ZSM; X-ray; 2.30 A; A/B/C=2-429.
DR PDBsum; 2EPJ; -.
DR PDBsum; 2ZSL; -.
DR PDBsum; 2ZSM; -.
DR AlphaFoldDB; Q9Y9I9; -.
DR SMR; Q9Y9I9; -.
DR STRING; 272557.APE_2299.1; -.
DR EnsemblBacteria; BAA81311; BAA81311; APE_2299.1.
DR KEGG; ape:APE_2299.1; -.
DR PATRIC; fig|272557.25.peg.1533; -.
DR eggNOG; arCOG00918; Archaea.
DR UniPathway; UPA00251; UER00317.
DR EvolutionaryTrace; Q9Y9I9; -.
DR Proteomes; UP000002518; 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"
FT /id="PRO_0000120476"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2EPJ"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2EPJ"
FT TURN 240..245
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2EPJ"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2EPJ"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 321..343
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2EPJ"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:2EPJ"
FT HELIX 409..427
FT /evidence="ECO:0007829|PDB:2EPJ"
SQ SEQUENCE 429 AA; 45954 MW; 6CC7C5A97EE1F65C CRC64;
MASGEKSRML FERTKELFPG GVNSPVRAAV KPYPFYVKRG EGAYLYTVDG ARIVDLVLAY
GPLILGHKHP RVLEAVEEAL ARGWLYGAPG EAEVLLAEKI LGYVKRGGMI RFVNSGTEAT
MTAIRLARGY TGRDLILKFD GCYHGSHDAV LVAAGSAAAH YGVPTSAGVP EAVARLTLVT
PYNDVEALER VFAEYGDRIA GVIVEPVIAN AGVIPPRREF LAALQRLSRE SGALLILDEV
VTGFRLGLEG AQGYFNIEGD IIVLGKIIGG GFPVGAVAGS REVMSLLTPQ GKVFNAGTFN
AHPITMAAGL ATLKALEEEP VYSVSREAAK ALEEAASEVL DRTGLPYTIN RVESMMQLFI
GVEEVSNAAQ ARKADKKFYV KLHEEMLRRG VFIAPSNLEA VFTGLPHQGE ALEIAVEGLR
SSLKTVLGS
