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Database: UniProt
Entry: M7NLY0_9MICC
LinkDB: M7NLY0_9MICC
Original site: M7NLY0_9MICC 
ID   M7NLY0_9MICC            Unreviewed;       387 AA.
AC   M7NLY0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Aminotransferase family, DegT/DnrJ/EryC1/StrS {ECO:0000313|EMBL:EMQ99548.1};
GN   ORFNames=ADIAG_00648 {ECO:0000313|EMBL:EMQ99548.1};
OS   Paeniglutamicibacter gangotriensis Lz1y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paeniglutamicibacter.
OX   NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ99548.1, ECO:0000313|Proteomes:UP000012015};
RN   [1] {ECO:0000313|EMBL:EMQ99548.1, ECO:0000313|Proteomes:UP000012015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz1y {ECO:0000313|EMBL:EMQ99548.1,
RC   ECO:0000313|Proteomes:UP000012015};
RX   PubMed=23766407;
RA   Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT   from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT   Station Dakshin Gangotri.";
RL   Genome Announc. 1:e00347-e00313(2013).
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:EMQ99548.1}.
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DR   EMBL; AOCK01000002; EMQ99548.1; -; Genomic_DNA.
DR   RefSeq; WP_007269855.1; NZ_AOCK01000002.1.
DR   AlphaFoldDB; M7NLY0; -.
DR   STRING; 1276920.ADIAG_00648; -.
DR   PATRIC; fig|1276920.7.peg.652; -.
DR   eggNOG; COG0399; Bacteria.
DR   Proteomes; UP000012015; 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:EMQ99548.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW   Transferase {ECO:0000313|EMBL:EMQ99548.1}.
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   387 AA;  42369 MW;  8679E0C80B320759 CRC64;
     MEQQAFLPFA LPDITEREIE AVVESMRSGW VTTGPKTAEF EKTMATFLGD SELHCVAVNS
     ATAGLHLAVE ALGLGPGDEV LVPTWTFTST AEVVRYVGAT PVFVDVEEST LNIDFDDAES
     KVNANTKAIM PVHFAGHSIS ADRIEKFASR HGLKVVEDAA HAFPATNGSS MVGNSSSDAV
     VFSFYATKTI TTGEGGLLVT RNADLAQRAR TMRLHGISRD VFARYTSKVP AWRYDVVAPG
     FKYNMTDIAA AMGVVQLSRA EEMRQNREAI AERYFEAFAG LPIGLPESGQ GLRHSWHLFV
     LRVGDAAPID RDKFIEDLAG LGVGTSVHFI PLHRHPYWRE TYNLSAFDFP IAERAFEQTV
     SLPIFSSMTE QQVDRVINAV KKVLAPA
//
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