ID A0A1G2E0P9_9BACT Unreviewed; 440 AA.
AC A0A1G2E0P9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2175_02400 {ECO:0000313|EMBL:OGZ18861.1};
OS Candidatus Nealsonbacteria bacterium RBG_13_42_11.
OC Bacteria; Candidatus Nealsonbacteria.
OX NCBI_TaxID=1801663 {ECO:0000313|EMBL:OGZ18861.1, ECO:0000313|Proteomes:UP000176755};
RN [1] {ECO:0000313|EMBL:OGZ18861.1, ECO:0000313|Proteomes:UP000176755}
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:OGZ18861.1}.
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DR EMBL; MHLY01000006; OGZ18861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2E0P9; -.
DR STRING; 1801663.A2175_02400; -.
DR Proteomes; UP000176755; Unassembled WGS sequence.
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; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 2.
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 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 440 AA; 50643 MW; D6A289396E0A02D1 CRC64;
MSKLISISLS PNVEKDDVLL AFKLIFQPWR WKKGKAIEEL EKEFKEYLDV KHAFSFNSGR
SSLMAILNSL GLEKDSEVLL QAFTCNAAVN PIIWTGLKPV FVDVNEKTFN MDAEDLRKKI
TLRRDSGQAP RVVMVQHTFG LSADMDEILE ICQKNNLILI EDCAHALGAK YKSKKVGLPA
DLSAEARRTE AETSAKAGTF GKAAFFSFSR DKVISSVYGG VAVTNDGDLA EKIKKYQEKS
GFPCYDWILQ QLLHPILMNW LVLPIYSIFG KYLLILFQWF QVLSKAVHWK EKRAMKPYYF
PKRLPNALAI LALNQFKKLE KFNRHRREIA NFYSRELLNT KYRIPDTKYL DSHIFLRFSI
KHPKAHEIIK NAWRKNLLIG DWYTTPIAPH DTKLDKMQYI SGSCPTAERL AKETLNLPTH
INISKEDAQR IVEFLKNYGN
//