ID A0A097IDN6_9CORY Unreviewed; 442 AA.
AC A0A097IDN6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375};
GN ORFNames=CDOO_02420 {ECO:0000313|EMBL:AIT60234.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT60234.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT60234.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT60234.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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:0000256|HAMAP-Rule:MF_00375};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|ARBA:ARBA00004819}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
CC {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
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DR EMBL; CP006764; AIT60234.1; -; Genomic_DNA.
DR RefSeq; WP_018021368.1; NZ_CP006764.1.
DR AlphaFoldDB; A0A097IDN6; -.
DR STRING; 558173.CDOO_02420; -.
DR KEGG; cdo:CDOO_02420; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_11; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000029914; 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:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:AIT60234.1};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00375};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00375}; Reference proteome {ECO:0000313|Proteomes:UP000029914};
KW Transferase {ECO:0000313|EMBL:AIT60234.1}.
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 442 AA; 45987 MW; DDFDC4B58E2FFD91 CRC64;
MTQPDVTSAH TGRSKELFDR ARTVTPGGVN SPVRAFGSVG GQARFIASAK GSRLTDVDGN
EYVDLVNSWG PMLNGNAREE ITAAVVDAAS RGLSFGAPTL GEIELAEEIV SRTSAEQVRL
VNSGTEATMS AVRLARGFTG RPKIIKFEGC YHGHVDALLA SAGSGVATFA LPDSPGVTGA
SAADTIVVPY NDVDAVRAAF AEHPGEIAAV ITEAAAGNMG TVAPREGFNA ALKEIAHENG
ALLILDEVMT GFRTSYRGWY GVDGVAGDLT TFGKVVSGGL PAAAFGGRRD IMEHLAPSGP
VYQAGTLSGN PVAVASGLAS LRLADESVYP VLHAHADRLS ALISEALTRE GVAHHMQRAS
TMLSVRFAEG EGHNFADMKA ADTFRFPAFY HALLDHGVYG PPSAYETWFV STALTDDDFE
KIEAALKPAA QAAAAAVADN EG
//
