ID Q4KE65_PSEF5 Unreviewed; 1015 AA.
AC Q4KE65;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Phosphotransferase family/peptidase, M23 family/aminotransferase, class III {ECO:0000313|EMBL:AAY91634.1};
GN OrderedLocusNames=PFL_2361 {ECO:0000313|EMBL:AAY91634.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91634.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY91634.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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|ARBA:ARBA00008954}.
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DR EMBL; CP000076; AAY91634.1; -; Genomic_DNA.
DR RefSeq; WP_011060661.1; NC_004129.6.
DR AlphaFoldDB; Q4KE65; -.
DR STRING; 220664.PFL_2361; -.
DR KEGG; pfl:PFL_2361; -.
DR PATRIC; fig|220664.5.peg.2405; -.
DR eggNOG; COG0160; Bacteria.
DR eggNOG; COG0739; Bacteria.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_010757_1_2_6; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd12797; M23_peptidase; 1.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAY91634.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:AAY91634.1}.
FT DOMAIN 37..270
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 443..543
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
SQ SEQUENCE 1015 AA; 111665 MW; 62D10F1B69050BD2 CRC64;
MTNLSHPAPQ FSPRDAEQLA EQLFNVVATA SPLDGERDCN YRLNTASDAG WILKVVNSSE
PRTESELQTA ILSHLASYNP ELAVPQLKKS LAGGFLASAV APSGETHAVR LVSWLHGTPL
AEVKRTFALM CSLGQSFADM DRALQGFMHP GAVRDLDWDL RHAARSRSRL HFVKDPGRRA
ILERFISAFE NTVQPRLARL RTQVIHNDGN DWNILVDPQT HQQVSGIIDF GDAVHTVLIA
EVAITCAYSI LDMEDPIGAA AALTAGFHER YPLQPQELDV LFNLIAMRLV ISVTLSASRH
EQTQDNPYLA ISEAPAWRLL EKMDRMNPRL ATAILRKACG YDAIEGAGAV RRWVDENRHA
FADIVHPAAA PLNKAIVPFA DAAHVLTVAS AEQRPAEAAK WWNDFAAEHQ VPLGIGPWGE
ERTIYTDAAF ESRFIAGQRR IIHLGVDLIM PAGTPLYTPL AGVVRSVEVE REPLGYGGLI
MLEHSPEGCP PFLTLWGHMA HEALTRLKPG DRLEAGALVG HMGADTENGG WLPHVHFQMS
TDTQLQASEF IGVGERAYLE VWADLFPDAS TLAGIPAETY SQEGRSKAEI VAKRKQLLLP
NLSISYSDPI KFVRGDGVWL IDNFGRAYLD CFNNVCHLGH SHPDVVQALA RQASRLNTNT
RYLHDNIVEY AERLTATLPE GLAVASFGCS GSEANSLMLR MARNHTGRND AIVLDWAYHG
TTQELIDLSP YKYKRKAGKG RAEHVFEAAV PDAYRAADHW PFEELGKRFA QSVAEQIDSM
RKQGRAPAFF LAESIPSVAG QLFFPENYLQ EVYAMVRAEG GLCLADEVQV GFGRVGSHWW
AFETQGVVPD AVSMGKPIGN GHPMSAVVTT REIADSFNNG MEYFNTFAGN PVSCAVGLSV
LDVIERDNLK LNALTVGNYL LDGFRTLQQR YDAIGDVRGL GLFLGIELVT DRKSKAPATQ
LARKVADGAR ERGILIGTEG PYDNVLKMRP SMIFSQKNAD FLLEVLDESF KAALR
//
