ID G8QUB1_SPHPG Unreviewed; 453 AA.
AC G8QUB1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=2,4-diaminobutyrate 4-transaminase {ECO:0000313|EMBL:AEV28081.1};
GN OrderedLocusNames=SpiGrapes_0218 {ECO:0000313|EMBL:AEV28081.1};
OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV28081.1, ECO:0000313|Proteomes:UP000005632};
RN [1] {ECO:0000313|EMBL:AEV28081.1, ECO:0000313|Proteomes:UP000005632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC {ECO:0000313|Proteomes:UP000005632};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA Loeffler F., Woyke T.;
RT "Complete sequence of Spirochaeta sp. grapes.";
RL Submitted (NOV-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; CP003155; AEV28081.1; -; Genomic_DNA.
DR RefSeq; WP_014268930.1; NC_016633.1.
DR AlphaFoldDB; G8QUB1; -.
DR STRING; 158190.SpiGrapes_0218; -.
DR KEGG; sgp:SpiGrapes_0218; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_12; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000005632; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000005632}.
SQ SEQUENCE 453 AA; 49349 MW; 0B7B00489F5B65CA CRC64;
MNEILQEKSN QYYLERQNNT ESNSRSYPRK FPFALKKAKG SWIEDVEGNK YLDFLCGAGT
LALGHNDSQV NQAMIDLLST DAPLHTLDLT TPVKDKFVHT LLNLLPGELK NNAKVQFCSP
SGTDAVDASL KLCKTATGRS SVIAFTGAYH GMGHGALSLT GNLSAKQKVN ALMPDVHFMP
YPYSYRCPFG IGGEAGVDAI CAYFERVLKD PESGITKPAA VILETIQGEG GVIPAPVKFL
QTVRRVTKEL GIPMIIDEIQ CGIGRSGKFF AFEYADIVPD VILASKAIGG TQPMAVVIYN
KDLDLWQPGA HAGTFRGNQL AMAAGTVVME RVSKPEFLQD VIEKGKIIED RLKGLMKEVS
ILGDIRSKGL MLGFEFVDPK GKPDQLGSLP ASGEIAAQVQ KECFNNHLIM EKGGRFGSVM
RCLCALNVSR EDIGIMLDIC EKVIRKVDAD AKR
//
