ID A0A045HUB4_MYCTX Unreviewed; 462 AA.
AC A0A045HUB4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 ECO:0000313|EMBL:SGI65693.1};
GN Synonyms=hemL2 {ECO:0000313|EMBL:OMH58407.1}, hemL_1
GN {ECO:0000313|EMBL:CKS10774.1};
GN ORFNames=A4S10_00556 {ECO:0000313|EMBL:OMH58407.1}, ERS027659_02650
GN {ECO:0000313|EMBL:CKS10774.1}, ERS027661_00538
GN {ECO:0000313|EMBL:CKR06710.1}, ERS053720_00010
GN {ECO:0000313|EMBL:CFH67231.1}, GJE03_02745
GN {ECO:0000313|EMBL:QGK77831.1}, SAMEA2683035_04072
GN {ECO:0000313|EMBL:SGI65693.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:SGI65693.1, ECO:0000313|Proteomes:UP000182946};
RN [1] {ECO:0000313|EMBL:CFH67231.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH67231.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH58407.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH58407.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGI65693.1, ECO:0000313|Proteomes:UP000182946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGI65693.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 185
RC {ECO:0000313|EMBL:CKS10774.1, ECO:0000313|Proteomes:UP000050164}, and
RC Bir 187 {ECO:0000313|EMBL:CKR06710.1,
RC ECO:0000313|Proteomes:UP000049023};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH58407.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH58407.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QGK77831.1, ECO:0000313|Proteomes:UP000388593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00018547 {ECO:0000313|EMBL:QGK77831.1,
RC ECO:0000313|Proteomes:UP000388593};
RA Baines S.L., Goncalves da Silva A., Carter G.P., Jennison A.V.,
RA Rathnayake I.U., Graham R.M.A., Sintchenko V., Wang Q., Rockett R.J.,
RA Timms V.J., Martinez E., Ballard S., Tomita T., Isles N., Horan K.A.,
RA Pitchers W., Stinear T.P., Williamson D.A., Howden B.P., Seemann T.;
RT "Complete microbial genomes for public health in Australia and Southwest
RT Pacific.";
RL Submitted (NOV-2019) 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; CFSW01000001; CFH67231.1; -; Genomic_DNA.
DR EMBL; CNFU01000066; CKR06710.1; -; Genomic_DNA.
DR EMBL; CNFT01000659; CKS10774.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH58407.1; -; Genomic_DNA.
DR EMBL; CP045962; QGK77831.1; -; Genomic_DNA.
DR EMBL; FPTZ01000051; SGI65693.1; -; Genomic_DNA.
DR RefSeq; WP_003402844.1; NZ_WUCS01000003.1.
DR PATRIC; fig|1773.211.peg.1235; -.
DR OMA; WGPLIFG; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000049023; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; Chromosome.
DR Proteomes; UP000388593; 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; 3.90.1150.10; 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 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}.
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:0000256|HAMAP-Rule:MF_00375"
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
//
