GSA_SYNE7
ID GSA_SYNE7 Reviewed; 433 AA.
AC Q31QJ2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=Synpcc7942_0645;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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 -!- 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=ABB56677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000100; ABB56677.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039755849.1; NC_007604.1.
DR PDB; 3USF; X-ray; 2.46 A; A/B=7-433.
DR PDBsum; 3USF; -.
DR AlphaFoldDB; Q31QJ2; -.
DR SMR; Q31QJ2; -.
DR STRING; 1140.Synpcc7942_0645; -.
DR PRIDE; Q31QJ2; -.
DR EnsemblBacteria; ABB56677; ABB56677; Synpcc7942_0645.
DR KEGG; syf:Synpcc7942_0645; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_3; -.
DR OrthoDB; 493793at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0645-MON; -.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR EvolutionaryTrace; Q31QJ2; -.
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-UniPathway.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..433
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243631"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:3USF"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3USF"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3USF"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 328..350
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:3USF"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:3USF"
FT HELIX 416..431
FT /evidence="ECO:0007829|PDB:3USF"
SQ SEQUENCE 433 AA; 46102 MW; 011176D3DF81275A CRC64;
MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA YAWDVDGNRY
IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE NVLAEMVIDA VPSIEMVRFV
NSGTEACMAV LRLMRAYTGR DKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKST
TANTLTAPYN DLEAVKALFA ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA
LLVFDEVMTG FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM
YQAGTLSGNP LAMTAGIKTL ELLRQPGTYE YLDQITKRLS DGLLAIAQET GHAACGGQVS
GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL APSQFEAGFT SLAHTEEDID
ATLAAARTVM SAL
