(data stored in ACNUC1104 zone)

SWISSPROT: GSA_NOCSJ

ID   GSA_NOCSJ               Reviewed;         445 AA.
AC   A1SE06;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=Noca_0499;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) 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; CP000509; ABL80041.1; -; Genomic_DNA.
DR   RefSeq; WP_011753991.1; NC_008699.1.
DR   SMR; A1SE06; -.
DR   STRING; 196162.Noca_0499; -.
DR   EnsemblBacteria; ABL80041; ABL80041; Noca_0499.
DR   KEGG; nca:Noca_0499; -.
DR   eggNOG; ENOG4105CDM; Bacteria.
DR   eggNOG; COG0001; LUCA.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000640; 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; A1SE06.
DR   SWISS-2DPAGE; A1SE06.
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    445       Glutamate-1-semialdehyde 2,1-aminomutase.
FT                                /FTId=PRO_0000382353.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00375}.
SQ   SEQUENCE   445 AA;  45631 MW;  65DB6E12442D2DF6 CRC64;
     MTAGATLPTA ASAALFERAR AVTPGGVNSP VRAFNAVGGT PRFIRSARGA WLTDADGNEY
     VDLICSWGPM LLGHAHPEVQ AAVSAAVARG TSYGAPTEPE VELAEEIAAR APVERVRFVS
     SGTEATMSAI RLARGFTGRD VVVKFAGCYH GHVDSLLASA GSGLATFAVP GTPGVPESST
     ALTLVLPYND RAAVEKAFAE HGDRIACLIT EAAPGNMGVV PPDADGSGGG FNGFLAETCA
     RHGALFVSDE VMTGFRASRQ GQWGLDGAVE GWRPDLMTFG KVMGGGFPAA AFGGRADVMS
     RLAPEGPVYQ AGTLSGNPIA TTAGLATLRL ATDDVYAHIG AAADTIKTAA SDALSRAGVE
     HVVQAAGTMF SVFLTAGPVR DFADASRTDV AAYAAFFHAM LDQGVYLPPS AYEAWFLSSA
     HDDRAVQTVL DALPTAARAA AAAQT
//

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