ID B3EHG1_CHLL2 Unreviewed; 379 AA.
AC B3EHG1;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Serine--glyoxylate transaminase {ECO:0000313|EMBL:ACD91323.1};
DE EC=2.6.1.45 {ECO:0000313|EMBL:ACD91323.1};
GN OrderedLocusNames=Clim_2300 {ECO:0000313|EMBL:ACD91323.1};
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD91323.1, ECO:0000313|Proteomes:UP000008841};
RN [1] {ECO:0000313|EMBL:ACD91323.1, ECO:0000313|Proteomes:UP000008841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330
RC {ECO:0000313|Proteomes:UP000008841};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP001097; ACD91323.1; -; Genomic_DNA.
DR RefSeq; WP_012467188.1; NC_010803.1.
DR AlphaFoldDB; B3EHG1; -.
DR STRING; 290315.Clim_2300; -.
DR KEGG; cli:Clim_2300; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_1_10; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000008841; Chromosome.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACD91323.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:ACD91323.1}.
FT DOMAIN 25..324
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 379 AA; 41334 MW; A8DF3E3D44FA7C0D CRC64;
MKKRLFTPGP TPVPENVMLR MAAPIIHHRN PEFMEILTRV HEDLKYLFRT TQPVVVLSCS
GTGGMEASVA SLFKSGEKVI TVNAGKFGER WGQLVRVFTG NCVEEKVQWG TAIQPERMAE
LLKEHPDAKG VCLTHSETST GTAADIKALC ALIREKSDAL ILVDGITAIG AHEFHFDDWG
ADICITGSQK GLMMPPGLAL VAISERAQDI INAHTHTQQF YLSLKKALKA HSAEDTPFTP
AVSLVIGLDE ALQMIKAEGI ENIWKRHESL AAACRQGCSA LGMKLFSNSP SFAVTPVWLP
EGVDWSAFNK ALKNKNGITV AAGQDEYKGK IFRVSHLGYY DELDMLTVIG GLERALKDIN
FDFEIGAGVS AVQKAFLGN
//
