(data stored in ACNUC10821 zone)

SWISSPROT: C8U1M4_ECO10

ID   C8U1M4_ECO10            Unreviewed;       426 AA.
AC   C8U1M4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375,
GN   ECO:0000313|EMBL:BAI29032.1};
GN   OrderedLocusNames=ECO103_0154 {ECO:0000313|EMBL:BAI29032.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29032.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29032.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_00375,
CC         ECO:0000256|SAAS:SAAS01124572};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00375,
CC         ECO:0000256|SAAS:SAAS01090802};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090801}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090808}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00375, ECO:0000256|SAAS:SAAS01090804}.
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DR   EMBL; AP010958; BAI29032.1; -; Genomic_DNA.
DR   RefSeq; WP_000045290.1; NC_013353.1.
DR   SMR; C8U1M4; -.
DR   EnsemblBacteria; BAI29032; BAI29032; ECO103_0154.
DR   KEGG; eoh:ECO103_0154; -.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; WGPLIFG; -.
DR   BioCyc; ECOL585395:ECO103_RS00790-MONOMER; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000959; 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:UniProtKB-KW.
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; C8U1M4.
DR   SWISS-2DPAGE; C8U1M4.
KW   Aminotransferase {ECO:0000313|EMBL:BAI29032.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090797};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090803};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090799};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS01090798};
KW   Transferase {ECO:0000313|EMBL:BAI29032.1}.
FT   MOD_RES     265    265       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00375}.
SQ   SEQUENCE   426 AA;  45356 MW;  D60FF032BF0DF7BA CRC64;
     MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG
     PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT ELVPTMDMVR MVNSGTEATM
     SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFAKHTLTCT
     YNDLASVRAA FEQYPQEIAC IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM
     TGFRVALAGA QDYYGVEPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG
     NPIAMAAGFA CLNEVAQPGV HETLDELTSR LAEGLLEAAE EAGIPLVVNH VGGMFGIFFT
     DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA GFMSVAHSME DINNTIDAAR
     RVFAKL
//

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