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Database: UniProt
Entry: E1ZB05_CHLVA
LinkDB: E1ZB05_CHLVA
Original site: E1ZB05_CHLVA 
ID   E1ZB05_CHLVA            Unreviewed;       456 AA.
AC   E1ZB05;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CHLNCDRAFT_34843 {ECO:0000313|EMBL:EFN57144.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN57144.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN57144.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; GL433840; EFN57144.1; -; Genomic_DNA.
DR   RefSeq; XP_005849246.1; XM_005849184.1.
DR   AlphaFoldDB; E1ZB05; -.
DR   STRING; 554065.E1ZB05; -.
DR   GeneID; 17356469; -.
DR   KEGG; cvr:CHLNCDRAFT_34843; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   InParanoid; E1ZB05; -.
DR   OrthoDB; 1107811at2759; -.
DR   Proteomes; UP000008141; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141}.
SQ   SEQUENCE   456 AA;  49312 MW;  332AC5B7F3033CD5 CRC64;
     MAIDRQRLRE LIEQEEATYL RTHRKSYELY KQAQTCLLAG VPMHWMVRSA GNFPITVTEG
     SGARFRCVDG HEYVDLCLGD TGAMAGHAPP TTSKAVAARA AAGITFMLPT EDAVWCGQEL
     TRRFGLKYWQ FALTATDANR FSIRLARHIT GRPKILVFNY CYHGSVEETF ITLRADGTPA
     LRAGNLGPPV DPRVTAKVVE FNDLAALEAA LAPGDVAAVL AEPAMTNIGI IHPDPGYHQA
     LREICTRTGT LLIIDETHTI CAGPGGYTRA HGLQPDIFVL GKPIAGGVPV AVYGFTEQLA
     ARLAGRIAVD ESDTGGIGGT LAGNALSLAA MRATLEHVLT EDAFRHTISL AQRFEAGVEG
     VIAAHGLPWI VKRLGCRVEY WFRPDPPRNG GEAAATVDAD LDRFMHLAAL NRGIMLTPFH
     NMALMAPTTT AADVDRHTAV FGECVELLLG RRPSRL
//
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