ID   F3ZMK6_9ACTN            Unreviewed;       477 AA.
AC   F3ZMK6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=STTU_5510 {ECO:0000313|EMBL:EGJ78297.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ78297.1};
RN   [1] {ECO:0000313|EMBL:EGJ78297.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ78297.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CM001165; EGJ78297.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3ZMK6; -.
DR   HOGENOM; CLU_017584_3_2_11; -.
DR   Proteomes; UP000003955; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.30.420.180; CobE/GbiG C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR002750; CobE/GbiG_C.
DR   InterPro; IPR036518; CobE/GbiG_C_sf.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF01890; CbiG_C; 1.
DR   SUPFAM; SSF159664; CobE/GbiG C-terminal domain-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          1..118
FT                   /note="CobE/GbiG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01890"
FT   DOMAIN          146..463
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   477 AA;  48936 MW;  1D3BDF350EAC8947 CRC64;
     MVGVGAATGA TAAEIEALVR GALGAAGLPL ARVRAVATVD RRAEAPAVVA LAARLGVPVR
     AYAPHELAAV SVPRPSRAPR AALGTGSVAE AAALAEAGGR GRLLVAKQKS ARATCAVAED
     PREGRVMPSY ELRHHGDAEV RGAGLTDLAV NVRAGTPPAW LRERLADALG SLAAYPDDRA
     ARAAVAARHG LAPERVLLTA GAAEAFVLLA RTLPVRRPVV VHPQFTEPEA ALRAAGHAVE
     RVLLREEDGF RLDPALVPAG ADLVVLGNPT NPTSVLHPAD VIASLARPGR TLVVDEAFVD
     TVPGERESLA SRTDVPGLLV LRSLTKTWGL AGLRIGYVLG APATLARLAR AQPLWPVSTP
     ALVAAEACSA PGALAEAEAA ARDLAGDRDF LAAGLAELPE ARVVGPASAS FLLVRLPGAA
     GVRERLRGAG WAVRRGDTFP GLGDEWLRVA VRDRGTSERF LAAVRGVVGA EMPGAGG
//