ID A0A258TWV8_9PROT Unreviewed; 380 AA.
AC A0A258TWV8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:OYY95900.1};
GN ORFNames=B7Y41_01045 {ECO:0000313|EMBL:OYY95900.1};
OS Hydrogenophilales bacterium 28-61-23.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY95900.1, ECO:0000313|Proteomes:UP000215898};
RN [1] {ECO:0000313|EMBL:OYY95900.1, ECO:0000313|Proteomes:UP000215898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-61-23 {ECO:0000313|EMBL:OYY95900.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYY95900.1}.
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DR EMBL; NCGJ01000001; OYY95900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258TWV8; -.
DR Proteomes; UP000215898; 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; 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 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 380 AA; 41472 MW; ED3DF14934F15706 CRC64;
MIPYGRQDIS SEDIAAVVAV LQSDWLTQGP AVPRFEKAVA NCCGARHAVA VNSATSALHL
ACLALGLGPG DSLWTTPNTF VASANCARYC GAEIDFVDID PHSLNLSPAA LAAKLAQAEK
AGKLPKVVVP VHFAGQSCDM SAINALAQRY GFRIVEDASH AIGGRYQDQP IGNGRYADIT
VFSFHPVKIV TTGEGGMALT NDPRLAERMA RLRSHGIARD AAAQAAHGPW YYEQVELGFN
YRMTDLQAAL GESQLRRLDR FVDARRRLAD RYDRLLADLP LTTPWRDPAS ASAWHLYVIR
LHAASRRRAV FEQLRAAGIG VNVHYIPVHL QPDYRRLGFS AGDFPVAEDY YVRAITLPLY
PGLSDTEQDR VVAALREALA
//
