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Database: UniProt/TrEMBL
Entry: D6Y3G8_THEBD
LinkDB: D6Y3G8_THEBD
Original site: D6Y3G8_THEBD 
ID   D6Y3G8_THEBD            Unreviewed;       432 AA.
AC   D6Y3G8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   19-FEB-2014, entry version 30.
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-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       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   OMA; CSWGPLI; -.
DR   BioCyc; TBIS469371:GHSI-273-MONOMER; -.
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-HAMAP.
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   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   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00713; hemL; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   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
//
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