ID D9XDI9_STRVT Unreviewed; 556 AA.
AC D9XDI9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putrescine aminotransferase {ECO:0000313|EMBL:EFL30368.1};
GN ORFNames=SSQG_00886 {ECO:0000313|EMBL:EFL30368.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL30368.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; GG657757; EFL30368.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XDI9; -.
DR STRING; 591159.SSQG_00886; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR InterPro; IPR005814; Aminotrans_3.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EFL30368.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW Transferase {ECO:0000313|EMBL:EFL30368.1}.
SQ SEQUENCE 556 AA; 60422 MW; FD1AF086BBEBA0F7 CRC64;
MTARWNGGKR ISARSAGARA FRAEKELDMN PELAVTELAE PYLRGLLTSA GLDVEYVRGE
GNTLYRLDAK GQETPVLDYA GGYGSLIFGH NNPEIVARAR ELVDGGVPVH AQFSFHPYAN
RLAAELNRII HRELGTDEPY YATFANSGAE AVEAAVKHAE LDRVLRVSET LEELAAGVER
ARTAVDDGSA TVPDAVYAQL ATERPADDPL APVIDEITRR NGERAAQAPV FLALEGGFHG
KLMGSVQLTH NEAYRAPFAA LGVRARFVPR GRPEALDEVL AQERGVLLGL TVEDGEVRVV
EREHPVFCAF LLEPIQGEGG IQVLSDEDAR IIQEFADATD CPLIIDEIQS GLGRTGTLLA
SSQTGLRGDY YTLAKSLGGG LAKASVMLVR QTRYRAQFEL VHSSTFAKDA FSCYLALKVL
EMLERDGGRA YRQATERGAA LQATLEKVRT AFPDVAKDVR GRGLMLGFEF HDQSEAEHPA
IREAAAGGLF GYVIAGHLLN RHSIRTFPTA SAVNTLRFEP SVLLTDEEIG RLEEALTDVC
VILREQAGER LVLSSS
//