GSA_MYCTO
ID GSA_MYCTO Reviewed; 462 AA.
AC P9WMN8; L0T413; O06390; P63506;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; OrderedLocusNames=MT0546;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK44769.1; -; Genomic_DNA.
DR PIR; G70544; G70544.
DR RefSeq; WP_003402844.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMN8; -.
DR SMR; P9WMN8; -.
DR EnsemblBacteria; AAK44769; AAK44769; MT0546.
DR KEGG; mtc:MT0546; -.
DR PATRIC; fig|83331.31.peg.578; -.
DR HOGENOM; CLU_016922_1_5_11; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000001020; 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: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..462
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000427271"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 47516 MW; 6DF950736EE2BFAA CRC64;
MGSTEQATSR VRGAARTSAQ LFEAACSVIP GGVNSPVRAF TAVGGTPRFI TEAHGCWLID
ADGNRYVDLV CSWGPMILGH AHPAVVEAVA KAAARGLSFG APTPAETQLA GEIIGRVAPV
ERIRLVNSGT EATMSAVRLA RGFTGRAKIV KFSGCYHGHV DALLADAGSG VATLGLCDDP
QRPASPRSQS SRGLPSSPGV TGAAAADTIV LPYNDIDAVQ QTFARFGEQI AAVITEASPG
NMGVVPPGPG FNAALRAITA EHGALLILDE VMTGFRVSRS GWYGIDPVPA DLFAFGKVMS
GGMPAAAFGG RAEVMQRLAP LGPVYQAGTL SGNPVAVAAG LATLRAADDA VYTALDANAD
RLAGLLSEAL TDAVVPHQIS RAGNMLSVFF GETPVTDFAS ARASQTWRYP AFFHAMLDAG
VYPPCSAFEA WFVSAALDDA AFGRIANALP AAARAAAQER PA