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
//