ID   A0A1C4WZ44_MICVI        Unreviewed;       414 AA.
AC   A0A1C4WZ44;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Putrescine aminotransferase {ECO:0000313|EMBL:SCF01483.1};
GN   ORFNames=GA0074695_2875 {ECO:0000313|EMBL:SCF01483.1};
OS   Micromonospora viridifaciens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1881 {ECO:0000313|EMBL:SCF01483.1, ECO:0000313|Proteomes:UP000198242};
RN   [1] {ECO:0000313|EMBL:SCF01483.1, ECO:0000313|Proteomes:UP000198242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43909 {ECO:0000313|EMBL:SCF01483.1,
RC   ECO:0000313|Proteomes:UP000198242};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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 class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; LT607411; SCF01483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4WZ44; -.
DR   Proteomes; UP000198242; Chromosome i.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:SCF01483.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SCF01483.1}.
SQ   SEQUENCE   414 AA;  43832 MW;  4764F6DECDF19CDF CRC64;
     MSSTVFDLYR RHLGEGLGRV AAMLHTPLEV GATGTVVHTA DGRQLLNCAG YGVFFVGAGN
     PVVLAAVRDQ LERQALSTRV LLNEPAARAA AALTSVAPEG LVKVHFANSG AEAVETAIKI
     ARANGRHRLV SMHSGYHGKT VGALSLTARS LYQDPFRPLL PEVTHVRFGD LDELAAVVDR
     DVCVVVEPVQ SEGGVIIPQP GYLKAVEALC RDRGAMLVLD EVMTGLGRLG TWWAADRDGV
     RPDVLLVGKA LSGGLVPVAA TLATEEAFAP FDKDPYLHTS TFSANPLAMA AVRATVEVIR
     EEKLVERAAD LGARLLAAIT ETVRSIGHLV ADVRGAGLLI GVEFRSGMHA AEFLMDLLDN
     DVVVNHSMNA HPVLRLTPPA TMTADEEKRL VASFERACAA LAARFPATGS DAPA
//