(data stored in SCRATCH zone)

HOGENOM: SEBTE_1_PE1004

ID   SEBTE_1_PE1004                       STANDARD;      PRT;   434 AA.
AC   SEBTE_1_PE1004; D1AFK7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase; Short=GSA;
DE   EC=5.4.3 8;AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE   (SEBTE_1.PE1004).
GN   Name=hemL; OrderedLocusNames=Sterm_1024;
OS   SEBALDELLA TERMITIDIS ATCC 33386.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Sebaldella.
OX   NCBI_TaxID=526218;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SEBTE_1.PE1004.
CC       Sebaldella termitidis ATCC 33386, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:D1AFK7_SEBTE
CC   -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC       aminolevulinate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
CC   -!- GENE_FAMILY: HOG000020210 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D1AFK7; -.
DR   EMBL; CP001739; ACZ07892.1; -; Genomic_DNA.
DR   RefSeq; YP_003307823.1; NC_013517.1.
DR   ProteinModelPortal; D1AFK7; -.
DR   GeneID; 8596503; -.
DR   GenomeReviews; CP001739_GR; Sterm_1024.
DR   KEGG; str:Sterm_1024; -.
DR   OMA; NANIPFF; -.
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:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
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_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2.
DR   PANTHER; PTHR11986; Aminotrans_3; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR00713; HemL; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   HOGENOMDNA; SEBTE_1.PE1004; -.
KW   glutamate-1-semialdehyde-2,1-aminomutase;
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate.
SQ   SEQUENCE   434 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNIKKSGEIF ERSQKSIPGG VNSPVRAFKS VDRQYPIFIE TAKGSRLYDV DGNEYTDCIG
     SWGPMLLGHN NERVLEAVKK SLDEGTSFGL PTEKEVELAE LIKECYPSID KVRLTTSGTE
     AAMAAVRLAR AYTQKNKIIK FEGCYHGHSD SLMVKAGSGL LTFGHQDSNG ITEGVMKDTI
     TLPFGNSEKL IEILDSEEEA ACIILEPVPA NMGLIIPEEG FLKLLREKCT EKNIVLIFDE
     VISGFRVSLG GAQELFNITP DLTVLGKIIG GGFPVGAFGG KKEIMDMVAP VGNVYHAGTL
     SGNPVSVSAG LETINILKEN REIYNTLEKR TKELVLRIEE LIEKYNIKAT VNHIGSLYTI
     FFSDKKVENL EDAMATDDKA YNTYFSSMLE DGIIVPPSKY EAHFISWAHN NEDFEKLIAG
     VEKSFIAINQ NSGR
//

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