GSA_DECAR
ID GSA_DECAR Reviewed; 427 AA.
AC Q478V1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=Daro_3902;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ48630.1; -; Genomic_DNA.
DR RefSeq; WP_011289625.1; NC_007298.1.
DR AlphaFoldDB; Q478V1; -.
DR SMR; Q478V1; -.
DR STRING; 159087.Daro_3902; -.
DR EnsemblBacteria; AAZ48630; AAZ48630; Daro_3902.
DR KEGG; dar:Daro_3902; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_4; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT CHAIN 1..427
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243567"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 427 AA; 44639 MW; 241B6995104C5F37 CRC64;
MTSRNQQLFE RAQRHIPGGV NSPVRAFRSV GGTPCFFQKG VGAKVQDADG KWYTDYVGSW
GPMILGHAHP DVIAAVQAAV VDGLSFGAPT EKEVDIADLL CELVPSMDMV RLVSSGTEAT
MSAIRLARGH TGRDVLIKFE GCYHGHSDGL LVKAGSGLLT FGNPSSSGVP AGTAETTMVL
TYNDPQELAD AFAKHGDKIA AVIVEPVVGN MNLIAPTQAF LNAMRDLCTK NGSVLIFDEV
MTGFRVGLKS AQGLFGITPD LSTFGKVVGG GMPLGAFGGK REIMEKIAPL GPVYQAGTLS
GNPIATAAGL ATLKLIQAPG FYEALTAKTK ALCDGLVAAA KKHGVAFSAQ NIGGMFGLYF
AEQCPGTYDE VLACDKEAFN RFFHAMLDAG HYFAPSAFEA GFVSAAHSDA DIAGTIAAAD
AYFASLK