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Database: UniProt
Entry: A5G9C0
LinkDB: A5G9C0
Original site: A5G9C0 
ID   GSA_GEOUR               Reviewed;         427 AA.
AC   A5G9C0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-SEP-2014, entry version 56.
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;
DE            Short=GSA-AT;
GN   Name=hemL; OrderedLocusNames=Gura_4245;
OS   Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Shelobolina E., Aklujkar M., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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 (Potential).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
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DR   EMBL; CP000698; ABQ28388.1; -; Genomic_DNA.
DR   RefSeq; WP_011941019.1; NC_009483.1.
DR   RefSeq; YP_001232961.1; NC_009483.1.
DR   ProteinModelPortal; A5G9C0; -.
DR   SMR; A5G9C0; 1-423.
DR   STRING; 351605.Gura_4245; -.
DR   EnsemblBacteria; ABQ28388; ABQ28388; Gura_4245.
DR   GeneID; 5165426; -.
DR   KEGG; gur:Gura_4245; -.
DR   PATRIC; 22038949; VBIGeoUra13052_4521.
DR   eggNOG; COG0001; -.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; AKHTIVL; -.
DR   OrthoDB; EOG6QVRHN; -.
DR   BioCyc; GURA351605:GI6A-4300-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.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    427       Glutamate-1-semialdehyde 2,1-aminomutase.
FT                                /FTId=PRO_1000079924.
FT   MOD_RES     267    267       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   427 AA;  45437 MW;  B1578D8B649DA55B CRC64;
     MNYSRSELLF QEAQKAIPGG VNSPVRAFKS VGTDPLFIEK ASGSRIYDVD GNEFIDYVGS
     WGPMILGHCH PQVVAAVKSA VDNGCSFGAP TELEITLAEM VIEAVPSIEM VRMVSSGTEA
     TMSAIRLARG YTGRDKILKF SGCYHGHSDS LLVKAGSGAA TFGVPDSPGV PQDFAKHTLT
     ATYNDLESVN KLVAENKNQI SCIIVEPVAG NMGTVPPREG FLEGLRSLCT EEGIVLIFDE
     VMSGFRVAYG GAQELYNVTP DMTTLGKIIG GGLPVGAFGG KKEIMSLLSP SGGVYQAGTL
     SGNPLAMTAG IETLKLLQTE GFYQDLDRKS DYVASGIAKA AKDAGFPIYS TRVGSMFCAF
     FSKKPVYDWT SAAACDTKAF AKYFRLMLDE GIYLAPSQFE TAFVSIAHST DDLDKTIAAA
     AKAFKSL
//
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