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Database: UniProt
Entry: A0A0Q9Y4H1_9STAP
LinkDB: A0A0Q9Y4H1_9STAP
Original site: A0A0Q9Y4H1_9STAP 
ID   A0A0Q9Y4H1_9STAP        Unreviewed;       403 AA.
AC   A0A0Q9Y4H1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Aminotransferase V {ECO:0000313|EMBL:KRG10977.1};
GN   ORFNames=ACA31_01315 {ECO:0000313|EMBL:KRG10977.1};
OS   Staphylococcus sp. NAM3COL9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1667172 {ECO:0000313|EMBL:KRG10977.1, ECO:0000313|Proteomes:UP000051126};
RN   [1] {ECO:0000313|EMBL:KRG10977.1, ECO:0000313|Proteomes:UP000051126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA309 {ECO:0000313|EMBL:KRG10977.1,
RC   ECO:0000313|Proteomes:UP000051126};
RA   Gaiero J., Nicol R., Habash M.;
RT   "Genome sequencing project of Staphylococcus sp. NA309.";
RL   Submitted (JUN-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         ECO:0000256|PIRSR:PIRSR000524-50};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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:KRG10977.1}.
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DR   EMBL; LGPC01000006; KRG10977.1; -; Genomic_DNA.
DR   RefSeq; WP_057511587.1; NZ_LGPC01000006.1.
DR   AlphaFoldDB; A0A0Q9Y4H1; -.
DR   PATRIC; fig|1667172.3.peg.267; -.
DR   OrthoDB; 389074at2; -.
DR   Proteomes; UP000051126; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KRG10977.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Transferase {ECO:0000313|EMBL:KRG10977.1}.
FT   DOMAIN          31..345
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   403 AA;  45040 MW;  D04B3BD5A718EDFD CRC64;
     MDDLKVNKRL IMTPGPVSVD PRVSQAMSNS ILGQFDYEFI DIMNKTMELI RKSFLTNNKW
     SFPIDGTSRA GLEAVIASIV KPGDTILVPI IGRFGYLFTE LVTRAGGIVH NIQKPVGEVF
     DQAEIIAALD TVKPKVLAIV HGETSTGRLQ PIDQLGRACK ERGIYSVVDA VATYQGMVIP
     VDEWELDSVI GGAQKCLSIP SGITPITFNK RFSDEINKRK RVELGIRSNE NTEQDTFIRS
     NYLDLTQLQD YWSPKRLNHH TESTTSIYAL YTGLKLALTE GIEVRAKRHA YHQEGLKSAL
     KVLGLEIFGD ETNEMKMIIC VNIPEGIDDN KFREGLLKNY GIEIAGSFGE LQGKIWRIGI
     MGYAIEKQNI LTFLSIFSLY LAHQGVQNLN SEKAIDTLLT YYS
//
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