ID D6Y3G8_THEBD Unreviewed; 432 AA.
AC D6Y3G8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 01-MAY-2013, entry version 24.
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;
GN Name=hemL; OrderedLocusNames=Tbis_0266;
OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 /
OS JCM 10125 / NBRC 14880 / R51).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Pseudonocardineae; Pseudonocardiaceae; Thermobispora.
OX NCBI_TaxID=469371;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 /
RC R51;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Thermobispora bispora DSM 43833.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC aminolevulinate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis.
CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
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DR EMBL; CP001874; ADG86997.1; -; Genomic_DNA.
DR RefSeq; YP_003650890.1; NC_014165.1.
DR ProteinModelPortal; D6Y3G8; -.
DR EnsemblBacteria; ADG86997; ADG86997; Tbis_0266.
DR GeneID; 9166742; -.
DR KEGG; tbi:Tbis_0266; -.
DR PATRIC; 38283424; VBITheBis80272_0269.
DR HOGENOM; HOG000020210; -.
DR KO; K01845; -.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:HAMAP.
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:HAMAP.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR PANTHER; PTHR11986:SF5; PTHR11986:SF5; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
PE 3: Inferred from homology;
KW Chlorophyll biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW Porphyrin biosynthesis; Pyridoxal phosphate.
FT MOD_RES 266 266 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 432 AA; 45337 MW; 20CA78F2DF87CEE2 CRC64;
MTRTQTSEAL FDRAKKIVPG GVNSPVRAFG AVGGTPRFMA SGEGPYLVDV DGNRYVDLVC
SWGPLILGHR HAAVVQAVEE ALSRGLSYGT ATEGEVLLAE EIVSRMPPVE KIRLVSSGTE
ATMSAVRLAR GFTGRSKVIK FAGCYHGHVD ALLASAGSGV ATFGLPDSPG VTGAAAADTI
VLPYNSVEAV EEAFRKFEIA CVITEACPAN MGVVPPAEGF NRRLRELCSE HGALLIIDEV
LTGFRVTAQG WYGVDPVDAD LMTFGKVMGG GLPAAAFGGR ADVMAHLAPE GPVYQAGTLS
GNPLAVAAGL ATLRACDQAV YDRLDRVAET IGRAASEALS AAGVPHRLQR AGNLFSIFFT
DRPVVDYESA RAQDTAAYRA FFHSMLDQGV YLPPSAFEAW FVSAAHDDEA VNRVLEALPA
AARAAAQAAR QG
//
