(data stored in ACNUC7421 zone)

HOGENOM: SHELP_1_PE1010

ID   SHELP_1_PE1010                       STANDARD;      PRT;   428 AA.
AC   SHELP_1_PE1010; A3QBN5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase; Short=GSA;
DE   EC=5.4.3 8;AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE   Short=GSA-AT; (SHELP_1.PE1010).
GN   Name=hemL; OrderedLocusNames=Shew_1012;
OS   SHEWANELLA LOIHICA PV-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHELP_1.PE1010.
CC       Shewanella loihica PV-4, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:GSA_SHELP
CC   -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC       aminolevulinate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC       aminolevulinate from L-glutamyl-tRNA(Glu): step 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.
CC   -!- GENE_FAMILY: HOG000020210 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A3QBN5; -.
DR   EMBL; CP000606; ABO22883.1; -; Genomic_DNA.
DR   RefSeq; YP_001093142.1; NC_009092.1.
DR   ProteinModelPortal; A3QBN5; -.
DR   SMR; A3QBN5; 2-422.
DR   STRING; A3QBN5; -.
DR   GeneID; 4921308; -.
DR   GenomeReviews; CP000606_GR; Shew_1012.
DR   KEGG; slo:Shew_1012; -.
DR   NMPDR; fig|323850.3.peg.308; -.
DR   eggNOG; COG0001; -.
DR   OMA; TYNDLDS; -.
DR   PhylomeDB; A3QBN5; -.
DR   ProtClustDB; PRK00062; -.
DR   BioCyc; SLOI323850:SHEW_1012-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:UniProtKB-KW.
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_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2.
DR   PANTHER; PTHR11986; Aminotrans_3; 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.
DR   HOGENOMDNA; SHELP_1.PE1010; -.
KW   glutamate-1-semialdehyde aminotransferase;
KW   Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate.
SQ   SEQUENCE   428 AA;  UNKNOWN MW;  UNKNOWN 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
//

If you have problems or comments...

PBIL Back to PBIL home page