ID C5D575_GEOSW Unreviewed; 443 AA.
AC C5D575;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACS23301.1};
GN OrderedLocusNames=GWCH70_0379 {ECO:0000313|EMBL:ACS23301.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS23301.1};
RN [1] {ECO:0000313|EMBL:ACS23301.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS23301.1};
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., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP001638; ACS23301.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D575; -.
DR STRING; 471223.GWCH70_0379; -.
DR KEGG; gwc:GWCH70_0379; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_1_9; -.
DR OrthoDB; 9807885at2; -.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:ACS23301.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ACS23301.1}.
SQ SEQUENCE 443 AA; 49041 MW; E72918A92B877C8E CRC64;
MNNQPLLTVD LVELDKKHFI HPTSSIKEQQ ENGPAAIFKE GHGVYVTDIN GKTYIEGMAS
LWNVNVGYGR KELAEAAKEQ MEKLAFSSCF ATFSNEPAIR LAAKLAEITP GDLSAVFFTS
GGSESNDTAY KLVRHYWKLK GYPNKTKIIS RKKAYHGVAI GATSATGIQD FQNMTTALAP
EFIHADTFSV DSVREIIERE GAENIAAFLA EPIQGAGGVN IPPDGYFQEI RKICDENNIL
FIADEVITGF GRTGKMFACE HWNVVPDVML IAKGITSGYI PLGAVIIHEK LHKDLIELSE
GTLLHGFTYS GHPTACAVAL RNIQIIEEEN LVENSRLMGE ELHKQLKMLQ SELPIVGEVR
SLGLIGALEI VKDKQTNERF EKKLAPIIIN EARQRGLILR TVTFGDADTI VFSPPLVINK
QEIQKMFQIL RDSMISVMNN LQI
//
