UniProt: A0A098TJT8

Database: UniProt
Entry: A0A098TJT8_9CYAN

LinkDB:  A0A098TJT8_9CYAN 
Original site:  A0A098TJT8_9CYAN

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
All databases (17)   

Download RDF

ID   A0A098TJT8_9CYAN        Unreviewed;       432 AA.
AC   A0A098TJT8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
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   ORFNames=DO97_07775 {ECO:0000313|EMBL:KGF72564.1};
OS   Neosynechococcus sphagnicola sy1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC   Neosynechococcaceae; Neosynechococcus.
OX   NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF72564.1, ECO:0000313|Proteomes:UP000030170};
RN   [1] {ECO:0000313|EMBL:KGF72564.1, ECO:0000313|Proteomes:UP000030170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF72564.1,
RC   ECO:0000313|Proteomes:UP000030170};
RA   Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT   "Evolution of Synechococcus.";
RL   Mol. Ecol. 0:0-0(2014).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00375};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
CC       {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGF72564.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JJML01000024; KGF72564.1; -; Genomic_DNA.
DR   RefSeq; WP_036533479.1; NZ_JJML01000024.1.
DR   AlphaFoldDB; A0A098TJT8; -.
DR   STRING; 1497020.DO97_07775; -.
DR   OrthoDB; 9807885at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000030170; Unassembled WGS sequence.
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:0015995; P:chlorophyll biosynthetic process; 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:KGF72564.1};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00375};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00375}; Reference proteome {ECO:0000313|Proteomes:UP000030170};
KW   Transferase {ECO:0000313|EMBL:KGF72564.1}.
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   432 AA;  46074 MW;  32A4C8D24FC7A619 CRC64;
     MISTTLKTTK SEEIFTTAQK LMPGGVSSPV RAFKSVGGQP IVFDRVQGAY LWDVDGNQYI
     DYVGSWGPAI CGHAHPVVIK ALQEALEKGT SFGAPCVLEN TLAEMVIDAV PSIEMVRFVN
     SGTEACMSVL RLMRAFTGRE KIIKFEGCYH GHADMFLVKA GSGVATLGLP DSPGVPKSTT
     SSTLTAPYNN LEAVKVLFDQ HPDQIAGVIL EPVVGNAGFI PPDVGFLAGL RELTQEYGAL
     LVFDEVMTGF RIAYGGAQEK FGITPDLTTL GKVIGGGLPV GAYGGRREIM ALVAPAGPMY
     QAGTLSGNPL AMTAGIKTLE LLRQPGTYEH LDRISGKLVA GLLQIARDAD HRVCGGHISG
     MFGLFFTPGP VHSYEDAKKS DLAKFSRFHR GMLEQGIYLA PSQFEAGFTS LAHTDAEIDR
     TLEAAQIVLS SF
//

DBGET integrated database retrieval system