ID Q1QEC9_PSYCK Unreviewed; 378 AA.
AC Q1QEC9;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:ABE73974.1};
GN OrderedLocusNames=Pcryo_0190 {ECO:0000313|EMBL:ABE73974.1};
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE73974.1, ECO:0000313|Proteomes:UP000002425};
RN [1] {ECO:0000313|Proteomes:UP000002425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5
RC {ECO:0000313|Proteomes:UP000002425};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP000323; ABE73974.1; -; Genomic_DNA.
DR RefSeq; WP_011512563.1; NC_007969.1.
DR AlphaFoldDB; Q1QEC9; -.
DR STRING; 335284.Pcryo_0190; -.
DR KEGG; pcr:Pcryo_0190; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_044792_0_0_6; -.
DR Proteomes; UP000002425; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABE73974.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:ABE73974.1}.
FT DOMAIN 22..291
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 378 AA; 41275 MW; 026B94DCBF00B57F CRC64;
MTALRQDIDP NGLLEYSVVY TDRALNHMSK AFQEVMNDLL SNLKTVYNAE AAVIIPGSGT
YGMEAVARQL TIDEDCLIIR NGWFSYRWTQ ILEKGKFAKS STVLTAERTE ETEVPKPFAP
VDIETAVAKI KADKSAVVYA PHVETSSGII LSEDYIKALS AAVHSVGGLL VIDCIASGCV
WLDMKKLGID VLISAPQKGW SSTPCAGLVM LSDAAIKKVE TTESNCFSLD LKQWLTIMRA
YENGGHAYHA TMPTDSLRQF RDTILEAKEI GFDKLCDAQW ELGNRVRKVL ADKGIESVAA
KGFEAPGVVV SYTDRDDIHK GSAFAEAGLQ IAAGVPLKVG EPENFKTFRL GLFGLDKLTD
VDGAVERFEK ALDEVLAK
//
