(data stored in ACNUC7421 zone)

HOGENOM: DICZE_1_PE1015

ID   DICZE_1_PE1015                       STANDARD;      PRT;   426 AA.
AC   DICZE_1_PE1015; C6CNI8;
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   (DICZE_1.PE1015).
GN   Name=hemL; OrderedLocusNames=Dd1591_1037;
OS   DICKEYA ZEAE ECH1591.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICZE_1.PE1015.
CC       Dickeya zeae Ech1591 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6CNI8_DICZE
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; C6CNI8; -.
DR   EMBL; CP001655; ACT05909.1; -; Genomic_DNA.
DR   RefSeq; YP_003003388.1; NC_012912.1.
DR   ProteinModelPortal; C6CNI8; -.
DR   STRING; C6CNI8; -.
DR   GeneID; 8120310; -.
DR   GenomeReviews; CP001655_GR; Dd1591_1037.
DR   KEGG; dze:Dd1591_1037; -.
DR   OMA; TYNDLDS; -.
DR   ProtClustDB; PRK00062; -.
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; DICZE_1.PE1015; -.
KW   glutamate-1-semialdehyde aminotransferase;
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate.
SQ   SEQUENCE   426 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNKSESLYAA ARQLIPGGVN SPVRAFNGVG GVPLFIERAE GARLYDADGK SYIDYVGSWG
     PMILGHNHPA IRQAVIDAAE RGLSFGAPTE MEVKMAQLVT SLVPGMEMVR MVNSGTEATM
     SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFARHTLTCT
     YNDLGSVRAA FEQYPQAIAA IIVEPVAGNM NCIPPLPAFL PGLRALCDEF GALLIIDEVM
     TGFRVALGGA QAHYGVRPDL TCLGKIIGGG MPVGAFGGRR DVMEALAPTG PVYQAGTLSG
     NPIAMAAGFA CLSEVAKPGV HQKLTELTTQ LAEGLLAAAK TQQIPLVVNH VGAMFGIFFT
     DAAQVTCYQD ALKCDVERFK RFFHLMLDEG IYLAPSAFEA GFMSLAHSQQ DIEYTVDAAR
     RCFAKL
//

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