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Database: UniProt
Entry: A0A0Q7N665_9NOCA
LinkDB: A0A0Q7N665_9NOCA
Original site: A0A0Q7N665_9NOCA 
ID   A0A0Q7N665_9NOCA        Unreviewed;       873 AA.
AC   A0A0Q7N665;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KQY29172.1};
GN   ORFNames=ASD42_27255 {ECO:0000313|EMBL:KQY29172.1};
OS   Nocardia sp. Root136.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY29172.1, ECO:0000313|Proteomes:UP000051507};
RN   [1] {ECO:0000313|Proteomes:UP000051507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY29172.1, ECO:0000313|Proteomes:UP000051507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root136 {ECO:0000313|EMBL:KQY29172.1,
RC   ECO:0000313|Proteomes:UP000051507};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- 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:KQY29172.1}.
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DR   EMBL; LMFE01000012; KQY29172.1; -; Genomic_DNA.
DR   RefSeq; WP_056823205.1; NZ_LMFE01000012.1.
DR   AlphaFoldDB; A0A0Q7N665; -.
DR   STRING; 1736458.ASD42_27255; -.
DR   Proteomes; UP000051507; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SMART; SM00220; S_TKc; 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   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KQY29172.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:KQY29172.1}.
FT   DOMAIN          106..368
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|SMART:SM00220"
SQ   SEQUENCE   873 AA;  96884 MW;  D3F855CC14E6EF11 CRC64;
     MFRHLAKAVG YAALGAAEYS IGSVRLHRQD SREERRAHAI VDFLLRMGPI YIKIGQIAAT
     RSDLLPESWI DTLRVLQDDT PHMSEDRTRR AVEREIGAPL ASRFRSFDLV PIASASVAQV
     HIAELIDGRK VAVKLVKDSV PAQIQSSLRS LRSAVRVAHA VAWPVRYLDM PTRFDEVARL
     LRPQADMNHE ATQQRRIHAN FAGHPFVKVP AVFDEFVTER MLVMEYMAGI PGKDAATVGF
     PPERLAQRLQ DAIYTMLYMH GICHGDPHPG NVMFTTDGEV ILVDYGVTAE LTEDEKWGLS
     SFYYACSRKE WSVAVERFTR HFVVAAPTLA EYRAAYDAEM VQVLRQHFDI SNNRWSTVAY
     FNDVNSVLRR YDSQYTTTFT KVELVFLSGE GFATQIDPGI DIWSNARKFT DRYSPYMSAE
     VEQRFETEFQ EQMPASLAMR DRAQATLVAP THIDRYFFPS SFPVFVAEAA GGSVTDCDGN
     TFLDLSGGYG PHLLGYAHPV INAAIASGLD KGLVNGIGNT PELELAEKLV GAFPSAQKAV
     LCNSGTESVL FAIRMARGYR QRTRVAKFEG HYHGFSDQAM VSSWFRFSGA KDRPEPVAGT
     LGSDPATVAG TVVLQYGDIS GLDRLRAEAD QLACVLLEPM PTSVVTLNVE FLRELRALCT
     ELDIPLIFDE VVSGFRVAYG GAQVLADVHP DLTCLGKVIG GGLPCGAVIG KQYLIDMAKS
     SQDPFYDYEN KVFAGGTLSG NSLTCTAGLA VLNHLDSHPE IYPQLEENTR LLAQLMREAT
     ESRGIACRIN AEHSIFSLNF SHRPAGLYRE RMAGSNFKAT IALAYYMRKH YVYLPEMHSF
     LISAAHDVED LGQIAQAFEK SLDEMLADQL FVT
//
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