ID A0A0Q9KYF7_9BACL Unreviewed; 406 AA.
AC A0A0Q9KYF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:KRE46316.1};
GN ORFNames=ASG81_11975 {ECO:0000313|EMBL:KRE46316.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE46316.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE46316.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE46316.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRE46316.1}.
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DR EMBL; LMRV01000038; KRE46316.1; -; Genomic_DNA.
DR RefSeq; WP_056633931.1; NZ_LMRV01000038.1.
DR AlphaFoldDB; A0A0Q9KYF7; -.
DR STRING; 1736388.ASG81_11975; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 406 AA; 45883 MW; 324415405456D1FE CRC64;
MDKENRWSQL AIHGGRPVRN DFLPYGRQWL EEDDIEAVVN VLKSDYLTTG PKISEFESKL
AETVGAKFAV AFSNGTAALH AACFVAGIKI GDEVITTPMT FAASANCILY NGGIPVFADI
DSKTYNIHPD AVRKAVNEKT KAIIPVHFTG QPVDLDPILK IAKERGVVVI EDAAHALGAS
YKKKKIGSIS DMTMFSFHPV KHITTGEGGI ITTNSEEYYD KLVQFRTHGI IREPYKLNEN
QGPWYYEMHN LGFNYRMTDI QAGLGLSQLT KIDRFLERRK RIVSIYNEAF KSMEPYIRLP
YQMAHGVSSC HLYILHFDTK KLNVGRNEIY KALLSENIGV NVHYIPVHLH PYYQSLGFKR
GLCPVAEKVY EEIITIPLFA KMTEEDAQDV ITAIRKVLCY YSSKEF
//
