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Database: UniProt
Entry: C9LV93_SELS3
LinkDB: C9LV93_SELS3
Original site: C9LV93_SELS3 
ID   C9LV93_SELS3            Unreviewed;       430 AA.
AC   C9LV93;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EEX77215.1};
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:AEB99039.1};
DE            EC=5.4.3.8 {ECO:0000313|EMBL:AEB99039.1};
GN   OrderedLocusNames=Selsp_0057 {ECO:0000313|EMBL:AEB99039.1};
GN   ORFNames=SELSPUOL_01385 {ECO:0000313|EMBL:EEX77215.1};
OS   Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX77215.1, ECO:0000313|Proteomes:UP000003505};
RN   [1] {ECO:0000313|EMBL:EEX77215.1, ECO:0000313|Proteomes:UP000003505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX77215.1}, and ATCC 35185 / DSM
RC   20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEB99039.1, ECO:0000313|Proteomes:UP000011124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEB99039.1}, and ATCC 35185 / DSM
RC   20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Selenomonas sputigena DSM 20758.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002637; AEB99039.1; -; Genomic_DNA.
DR   EMBL; ACKP02000024; EEX77215.1; -; Genomic_DNA.
DR   RefSeq; WP_006192684.1; NZ_GG698597.1.
DR   AlphaFoldDB; C9LV93; -.
DR   STRING; 546271.Selsp_0057; -.
DR   KEGG; ssg:Selsp_0057; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_4_9; -.
DR   OrthoDB; 3034088at2; -.
DR   Proteomes; UP000003505; Unassembled WGS sequence.
DR   Proteomes; UP000011124; Chromosome.
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   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   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   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:EEX77215.1};
KW   Isomerase {ECO:0000313|EMBL:AEB99039.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011124};
KW   Transferase {ECO:0000313|EMBL:EEX77215.1}.
SQ   SEQUENCE   430 AA;  48398 MW;  A815A60ABBE0E9B9 CRC64;
     MEINKRSLEK SEELWQTAQD TILSGCQLYS KGPETHIKGV SPIYIDHGKG AHVWDLDGNE
     YIDYDMGLGP IILGYQYKAV DDAVRAQLQR GMGYSLVAPE EVEYAKLCVK HIPSAGKVRF
     LKTGSSATEA AVRIARCYTG RKHIVRGEYH GWHEWTTAAE SVRQGGILPE VRQFVHKFDY
     NDLAKVEEYF ETYKGEIAAV ITEAVEIEPP KEGFLKRLKE LCHRNGALLI FDEVVNGFRF
     SIGGAQAYFG VTPDLSTFGK AAANGMPLSI VAGRKDIMEE VDKSIFISTT FGGECLSLAA
     GIAVMKALES GEVTKAIWEK GKYLQDNFRR LAKELDVPID LSGYPCRLNL EYTDYEGRKD
     WLYNSIFMQE SVKRGVLLGW HIFPCYSHTQ EDLDFTLNVF EDAMKVYREA LKSGHPERYM
     EGQPLKIVLG
//
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