(data stored in ACNUC7421 zone)

SWISSPROT: GSA_SHELP

ID   GSA_SHELP               Reviewed;         428 AA.
AC   A3QBN5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=Shew_1012;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC         Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC         EC=5.4.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       2/2. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00375}.
DR   EMBL; CP000606; ABO22883.1; -; Genomic_DNA.
DR   RefSeq; WP_011864816.1; NC_009092.1.
DR   SMR; A3QBN5; -.
DR   STRING; 323850.Shew_1012; -.
DR   EnsemblBacteria; ABO22883; ABO22883; Shew_1012.
DR   KEGG; slo:Shew_1012; -.
DR   eggNOG; ENOG4105CDM; Bacteria.
DR   eggNOG; COG0001; LUCA.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   BioCyc; SLOI323850:G1G8D-1073-MONOMER; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001558; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
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   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00713; hemL; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3QBN5.
DR   SWISS-2DPAGE; A3QBN5.
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    428       Glutamate-1-semialdehyde 2,1-aminomutase.
FT                                /FTId=PRO_0000300947.
FT   MOD_RES     265    265       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00375}.
SQ   SEQUENCE   428 AA;  46071 MW;  735F1BD86EBE8A10 CRC64;
     MTRSETLFEQ AKKTIPGGVN SPVRAFNGVG GSPRFIEKAD GAYIYDADGK AYIDYVGSWG
     PMILGHNHPK IRQAVLDAVE NGLSFGAPTE LEVRMAEKVI EMVPSMEQVR MVSSGTEATM
     SAIRLARGFT NRDKILKFEG CYHGHADCLL VKAGSGALTL GQPSSPGIPE DFAKHTLTAV
     YNELESVKTL FEQYPEEIAC IILEPVAGNM NCIPPIPGFL EGLRALCDQY GALLIIDEVM
     TGFRVSKSGA QGHYGITPDL TTLGKVIGGG MPVGAFGGRK EVMQFIAPTG PVYQAGTLSG
     NPIAMSAGLA QMEELCAEGL YEELAAKTKR IAEGFKAAAN KHGIPLSINY VGGMFGFFFT
     ELEQVTRFDQ VTQCDAEAFR TFYHGMLDEG VYLAPSAYEA GFLSMAHGEK ELEETLAAAD
     RVFARMAK
//

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