ID   A0A1Q8BP77_9CYAN        Unreviewed;       332 AA.
AC   A0A1Q8BP77;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-NOV-2023, entry version 14.
DE   SubName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000313|EMBL:OLE97850.1};
DE   Flags: Fragment;
GN   ORFNames=AUG75_03375 {ECO:0000313|EMBL:OLE97850.1};
OS   Cyanobacteria bacterium 13_1_20CM_4_61_6.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1805100 {ECO:0000313|EMBL:OLE97850.1, ECO:0000313|Proteomes:UP000186597};
RN   [1] {ECO:0000313|EMBL:OLE97850.1, ECO:0000313|Proteomes:UP000186597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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:OLE97850.1}.
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DR   EMBL; MNIV01000466; OLE97850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8BP77; -.
DR   Proteomes; UP000186597; 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        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         127
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OLE97850.1"
SQ   SEQUENCE   332 AA;  37366 MW;  6D0B1E66FE40DE44 CRC64;
     CTHALEMTAL LLRLQPGDEV IVPSFTFTST ANAFALRGAR IVFADIRPDT LNLDERQVER
     LITNRTKAII VVHYAGVGCE MDVLLEVAKR HGVAVIEDNA HGLFGKYRGR YLGTFGDLAA
     QSFHETKNFS CGEGGALVIN EPKLIEDAEV IRENGTNRSR FFRGEIDKYS WIGLGSSYLP
     SDILAALLLS QLEARDEIQL RRQQIWQVYY AGLRQWAEQQ GVGLPFTPAY CDQAYHVFYL
     LLPSLEDRQA LISHLRSHGI LAVFHYLPLH LSEFGRQWGG KEGDCPVTED VSARLLRLPF
     FYSLADSEQA RIVDSICSFV PEDVRTRRAS MT
//