GSA_THEVB
ID GSA_THEVB Reviewed; 437 AA.
AC Q8DLK8;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=tlr0479;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {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=BAC08031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC08031.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681269.2; NC_004113.1.
DR PDB; 2CFB; X-ray; 2.85 A; A=27-437.
DR PDBsum; 2CFB; -.
DR AlphaFoldDB; Q8DLK8; -.
DR SMR; Q8DLK8; -.
DR STRING; 197221.22294200; -.
DR PRIDE; Q8DLK8; -.
DR EnsemblBacteria; BAC08031; BAC08031; BAC08031.
DR KEGG; tel:tlr0479; -.
DR PATRIC; fig|197221.4.peg.504; -.
DR eggNOG; COG0001; Bacteria.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR EvolutionaryTrace; Q8DLK8; -.
DR Proteomes; UP000000440; 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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
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; Chlorophyll biosynthesis; Cytoplasm; Isomerase;
KW Porphyrin biosynthesis; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..437
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120460"
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2CFB"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2CFB"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2CFB"
FT TURN 251..256
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 332..352
FT /evidence="ECO:0007829|PDB:2CFB"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2CFB"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:2CFB"
FT HELIX 420..434
FT /evidence="ECO:0007829|PDB:2CFB"
SQ SEQUENCE 437 AA; 46450 MW; 5FDD56F62A179C23 CRC64;
MRELTLTTTV FQTTKSQEIF AAAQKLMPGG VSSPVRAFKS VGGQPIVFDH VKGAHIWDVD
GNQYIDYVGS WGPAIVGHAH PEVIDALHAA LEKGTSFGAP CLLENILAEM VIAAVPSVEM
VRFVNSGTEA CMAVLRLMRA YTQREKVIKF EGCYHGHADM FLVKAGSGVA TLGLPDSPGV
PKATTAATLT APYNDLEAVS RLFEQYPNDI AGVILEPVVG NAGFIPPDAG FLEGLRELTK
QYGALLVFDE VMTGFRIAYG GAQEKFGVTP DLTTLGKVIG GGLPVGAYGG RAEIMKMVAP
AGPVYQAGTL SGNPLAMTAG IKTLEILSRP GSYEHLDRIT GKLVQGLLDA AREFGHEVCG
GHISGMFGLF FTAGPVTNYE QAKQSDLKKF AAFHRGMLEQ GIYLAPSQFE AGFTSLAHTE
ADIERTIAAA RTVLSQL
