ID GSA_RIPO1 Reviewed; 433 AA.
AC B7K2I1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=PCC8801_2361;
OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS 8801)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801 / RF-1;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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}.
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DR EMBL; CP001287; ACK66374.1; -; Genomic_DNA.
DR RefSeq; WP_012595642.1; NC_011726.1.
DR AlphaFoldDB; B7K2I1; -.
DR SMR; B7K2I1; -.
DR STRING; 41431.PCC8801_2361; -.
DR KEGG; cyp:PCC8801_2361; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_3; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000008204; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00713; hemL; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Chlorophyll biosynthesis; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..433
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_1000121876"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 433 AA; 46084 MW; DB0F131B5E221394 CRC64;
MVSTSSFQTT KSEEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKGA YIWDVDGNQY
IDYVGTWGPA ICGHAHPDVI AALHEALEKG TSFGAPSVQE NILAEMVIEA VPSIEMVRFV
NSGTEACMSV LRLMRAFTGR EKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKAT
TSFTLTAPYN DLEAVKALFA ENPDDIAGVI LEPVVGNSGF VLPDAGFLEG LRELTKEYGA
LLMFDEVMTG FRLAYGGAQE KFGVTPDLTT LGKVIGGGLP VGAYGGRQDI MEMVAPSGPM
YQAGTLSGNP LAMTAGIKTL ELLQKPGTYD YLNDITQKLA DGLLKLAQDA GHAVCGGHIG
AMFGLFLTAG PVHNYEDAKK SDLVKFGRFH RAMLERGVYL APSQFEAGFT SLAHTQADID
RTLAMAKEVF SHL
//
