ID B3T8I4_9ZZZZ Unreviewed; 428 AA.
AC B3T8I4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|ARBA:ARBA00012143};
DE EC=5.4.3.8 {ECO:0000256|ARBA:ARBA00012143};
GN ORFNames=ALOHA_HF4000APKG5H11ctg2g11 {ECO:0000313|EMBL:ABZ08893.1};
OS uncultured marine microorganism HF4000_APKG5H11.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=455550 {ECO:0000313|EMBL:ABZ08893.1};
RN [1] {ECO:0000313|EMBL:ABZ08893.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004819}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
CC {ECO:0000256|ARBA:ARBA00008981}.
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DR EMBL; EU016639; ABZ08893.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T8I4; -.
DR UniPathway; UPA00251; UER00317.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00713; hemL; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABZ08893.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:ABZ08893.1}.
SQ SEQUENCE 428 AA; 44569 MW; 454DE02C37804543 CRC64;
MQLSKSEALF AEAQKYIPGG VNSPVRSFKS VGGTPPFIAR GQGSRIWDVD GNEYIDYLGS
WGPLVLGHSH PAVVEVLKKT AESGTSFGAP VEQEVELAKI ICGALPSVES VRLVSSGTEA
CMSAIRLARA FTGRDKIIKF AGCYHGHADG LLVKAGSGAL THGIPTSAGV PASYASETLV
AEFNDIGSVE RFFEANPGGI AAIIIEPVAG NMGVVPPAAG FLESVRKITQ DNGALLIFDE
VITGFRVGPN GAQGLYGITP DITTLGKIIG GGLPVGAYGG RKDIMEMVAP LGAMYQAGTL
SGNPLAVNAG ITTLKELQKT GTYERLETLA QRLTDGLTKA FQAVEMPSTI NRVGSMFTGF
FNAGPVAGLA DAEGSDTEMY GRYFHAMQEQ GVYIAPSQFE AGFVSTAHTE ADIDATIAKA
GAALSTLR
//
