ID A0A0M8T7Q2_9ACTN Unreviewed; 443 AA.
AC A0A0M8T7Q2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0000313|EMBL:KOU51294.1};
GN ORFNames=ADK56_10680 {ECO:0000313|EMBL:KOU51294.1};
OS Streptomyces sp. MMG1522.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU51294.1, ECO:0000313|Proteomes:UP000037713};
RN [1] {ECO:0000313|EMBL:KOU51294.1, ECO:0000313|Proteomes:UP000037713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1522 {ECO:0000313|EMBL:KOU51294.1,
RC ECO:0000313|Proteomes:UP000037713};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KOU51294.1}.
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DR EMBL; LGDF01000105; KOU51294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8T7Q2; -.
DR PATRIC; fig|1415545.3.peg.2299; -.
DR Proteomes; UP000037713; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; 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; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KOU51294.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KOU51294.1}.
FT REGION 211..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 174
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 443 AA; 45705 MW; B9F5D2856675C7E5 CRC64;
MGEAELSAVA EVFADNWLGH GPRTAAFEAE FAAHLGVPAD RVVFLASATA GLYLTTELLG
LGPGDEVVMP SISFVSAASA VASTGARPVF CDVDPDTLNP SAEQIARALT DRTRAVLVLH
YGGGPGDIAR IAELCESRGV PLVEDTACAV ASRVGPRACG TFGSLSVWSF DAMKVLSTGD
GGMLYAADPV VAGRARRLAY HGLAQSSGLS AARNAAGGGP DAAGEAPDAA AGDRGAEADA
NGGGPDGTGT GPTSPRTAPG APAPQPGAAG ARVPSRWWDL DVRDFGRRVI GNDLTAAIGS
VQLRRLEAIV DRRGEVAAAY DRLLSPLAGV RLPPPLPPDH TTSYYFYWVR LDPRIRDAVA
SDLLGRGVYT TFRYPPLHRV PAYGHHGPPL PHTESAAEAT LLLPLHQGLS DADVATVAAE
FRASVEARTP ARPTGLPKEG VPA
//
