ID A0A3N2MPZ2_9BACT Unreviewed; 379 AA.
AC A0A3N2MPZ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:ROT12222.1};
GN ORFNames=EEL48_13065 {ECO:0000313|EMBL:ROT12222.1};
OS Muribaculaceae bacterium Isolate-102 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486470 {ECO:0000313|EMBL:ROT12222.1, ECO:0000313|Proteomes:UP000272558};
RN [1] {ECO:0000313|EMBL:ROT12222.1, ECO:0000313|Proteomes:UP000272558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-102 (HZI) {ECO:0000313|Proteomes:UP000272558};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT12222.1}.
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DR EMBL; RIBI01000008; ROT12222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2MPZ2; -.
DR Proteomes; UP000272558; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:ROT12222.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000272558};
KW Transferase {ECO:0000313|EMBL:ROT12222.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 379 AA; 42451 MW; 29A8545A3C2072B8 CRC64;
MKMVDLYSQY LSMRKEIDSA IMGVVASSDF IKGTEVALLE EELAEYIGVR HCITCGNGTD
ALILSLMAMD LMPGDEVIVP SFAFASIVEA VLLLGGVPVF TDVDNTTFNI DVKSVERVIS
DRTKAIVPVH LFGQPCNMLE LMEISRSHKI VVIEDNAQSF GALCRMESGK EIYAGGIGDI
SYTSFFPTKM LGCYGDGGAV FTNNDILAKR VRELSNHGQC YKYMHEMIGF NSRLDTMQAA
VLRVKLKHLS QSIRGRRMLA EHYSKLLSDI EDIELPVEVN YGKHVYHQYT IKTKPSMRDD
LKEMLMSRGI QSMVYYPMPL FEQPAYCGKG LCDPEMNICP SLCKSVLSLP MYGELTYGQQ
DEIAYAVKAY FNNHNVYKS
//