ID Q82Y54_NITEU Unreviewed; 405 AA.
AC Q82Y54;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Aminotransferase class-V {ECO:0000313|EMBL:CAD83945.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CAD83945.1};
GN OrderedLocusNames=NE0034 {ECO:0000313|EMBL:CAD83945.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD83945.1, ECO:0000313|Proteomes:UP000001416};
RN [1] {ECO:0000313|EMBL:CAD83945.1, ECO:0000313|Proteomes:UP000001416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000313|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA Whittaker M., Arp D.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; AL954747; CAD83945.1; -; Genomic_DNA.
DR RefSeq; WP_011110686.1; NC_004757.1.
DR AlphaFoldDB; Q82Y54; -.
DR STRING; 228410.NE0034; -.
DR KEGG; neu:NE0034; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_4; -.
DR OrthoDB; 9766472at2; -.
DR PhylomeDB; Q82Y54; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd06451; AGAT_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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAD83945.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW Transferase {ECO:0000313|EMBL:CAD83945.1}.
FT DOMAIN 42..344
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 405 AA; 44939 MW; D5BC4C8AB36710DA CRC64;
MTTESFRPEK KITTFYPPQR TLMGPGPSDT HPRVLSAMAR PTLGHLDPVF TEMMEELKGL
LRYVFQTTNL MTFPVSGPGS VGMEMCFVNM IVPGDKVVVC RNGVFGGRMI ENVERCGGIP
LVVEDKWGDP VDPQKVEDML KKNPDAKIVA FVHAETSTGV QSDARTIAQI ARKHDCLTIM
DTVTSLGGTP VYMDAWDIDA IYSGSQKCLS CPPGLSPVSF SERVVDLVRN RTEKVHSWFM
DISLLLGYWG ASRTYHHTAP TNSLYGLHES LVILYEEGLE RSWARHRRNH EALKAGLKTL
GIEYVVAEPY RLPQLNSVYV PAGVDEKEVR RRLLDSYNLE IGAGLGDFAG KIWRFGLMGN
SSKLENVVFC LDALEHVLID MGVKVNRGTA SSAAHQYYAT NPVLA
//
