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 29-MAY-2013, entry version 50.
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; 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; FNGNPIS; -.
DR ProtClustDB; PRK00062; -.
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: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.
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
//
