ID A0A1G1CPS2_9BACT Unreviewed; 359 AA.
AC A0A1G1CPS2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2W24_02375 {ECO:0000313|EMBL:OGV97014.1};
OS Microgenomates group bacterium RBG_16_45_19.
OC Bacteria.
OX NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV97014.1, ECO:0000313|Proteomes:UP000178440};
RN [1] {ECO:0000313|EMBL:OGV97014.1, ECO:0000313|Proteomes:UP000178440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV97014.1}.
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DR EMBL; MHDC01000014; OGV97014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1CPS2; -.
DR STRING; 1817747.A2W24_02375; -.
DR Proteomes; UP000178440; Unassembled WGS sequence.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 173
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 359 AA; 40479 MW; 4A943320D9F8FF31 CRC64;
MPVIPLLKPS PSPAEIKAVK RVLQSSWWGL GPVTAQLETA FAAFVGTTYA IAVNSCSAAL
HLSVHILSRR FPKKTNLVTT PLTFISTAAA GLYENLEVRF GDIEEQTLCL DPQDALAKAD
ALTLTIIPVH YAGILSPIPQ TPLPIIEDCA HAAGTPGAGH SSLLACWSFH PVKNIATGDG
GMITTNDRQL AAELRRLRWL GIDQDTWARE QKGYNWEYQI PSLGFKYHTN DIMSAIALEQ
LKRLPTLNRR RRRLAKRYRT GLKDLPLILP PPSGSWHLYP IRLHRASLRP RLIQYLRDHH
ISVGVHYQPL HHYPFFNWHQ PLPVTDRVYP TLLDLPIFPD MTLAEQDYVI HTLHDFYNL
//