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Database: UniProt
Entry: I7LND5_METBM
LinkDB: I7LND5_METBM
Original site: I7LND5_METBM 
ID   I7LND5_METBM            Unreviewed;       360 AA.
AC   I7LND5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=UDP-4-amino-4-deoxy-L-arabinoseaminotransferase {ECO:0000313|EMBL:CCJ36994.1};
DE            EC=2.6.1.87 {ECO:0000313|EMBL:CCJ36994.1};
GN   OrderedLocusNames=BN140_2071 {ECO:0000313|EMBL:CCJ36994.1};
OS   Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS   (Methanogenium bourgense).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36994.1, ECO:0000313|Proteomes:UP000009007};
RN   [1] {ECO:0000313|Proteomes:UP000009007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC   {ECO:0000313|Proteomes:UP000009007};
RX   PubMed=22965103; DOI=10.1128/JB.01292-12;
RA   Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA   Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT   "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT   Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT   digester.";
RL   J. Bacteriol. 194:5487-5488(2012).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; HE964772; CCJ36994.1; -; Genomic_DNA.
DR   RefSeq; WP_014867967.1; NC_018227.2.
DR   AlphaFoldDB; I7LND5; -.
DR   STRING; 1201294.BN140_2071; -.
DR   GeneID; 13355345; -.
DR   KEGG; mbg:BN140_2071; -.
DR   PATRIC; fig|1201294.9.peg.2278; -.
DR   HOGENOM; CLU_033332_7_2_2; -.
DR   BioCyc; MBOU1201294:BN140_RS10315-MONOMER; -.
DR   Proteomes; UP000009007; Chromosome.
DR   GO; GO:0099620; F:UDP-4-amino-4-deoxy-L-arabinose aminotransferase; IEA:UniProtKB-EC.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CCJ36994.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009007};
KW   Transferase {ECO:0000313|EMBL:CCJ36994.1}.
SQ   SEQUENCE   360 AA;  38125 MW;  3074B72B0A643522 CRC64;
     MQIPIAHPSL GNEENTAVLA VLASGMIAQG PETAAFEEEF AAYCGVPHAV ATNNGTAALH
     AALLAAGVGP GDEVVVPAFT FFATASSVSM CGARPVFADV DPATATIDPA DILAKVSPTT
     KAVIAVHLYG QPCDVGAVRE VCDDKDLVFI EDAAQAHGAT YRGQKTGSLG DLACFSFYAT
     KNMATGEGGM VTTGSDEYDE RLRRVINHGQ SEKYLHTELG YNYRMTDINA AIGRVQLAKL
     DGFNRRRQEN AAYYNTHITA PGLVLPAVAP GRTHVWHQYS LRVTDAFPLS RDELMAYLRE
     RGIGCAVHYP VALSRQPFYA GAASCPVAES LAASVLSIPV HPGVIDEARA YIADTINGVV
//
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