ID E3CZR2_9BACT Unreviewed; 382 AA.
AC E3CZR2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=Apau_2287 {ECO:0000313|EMBL:EFQ24694.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ24694.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ24694.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ24694.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CM001022; EFQ24694.1; -; Genomic_DNA.
DR RefSeq; WP_006301939.1; NZ_CM001022.1.
DR AlphaFoldDB; E3CZR2; -.
DR STRING; 584708.Apau_2287; -.
DR PaxDb; 584708-Apau_2287; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_0; -.
DR Proteomes; UP000005096; Chromosome.
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:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF3; ASPARTATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:EFQ24694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005096};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EFQ24694.1}.
FT DOMAIN 27..377
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 382 AA; 41649 MW; 0183B49A1B08855A CRC64;
MRPSAKCLSA PRSEIRTMFS LAAGYPDALS LGIGEPDFPT PEHIREAGKR ALDEGRTKYT
PNAGIPELRR GLAEKLSREN GLACDPERNL VVTSGACEAI MLSLLGLVEP GDEVLVPDPG
WPNYYGQVHM AGGTTVPYPL LESERFHVRA ERIAPRITPR TRLLLLNSPG NPTGAVTSPE
ELREVADLAI RHDLTVISDE PYEKFLYDGA RHLSPASLPG MAERVLTVNS FSKTYSMTGW
RVGYIHGPEE VVTELVKLQE GMSACVTACA QWAALEALRG SQDCTRVMVE AYRRRRDLLV
EGLNRLPGVH CILPEGAFYA FANVEVLGSS QEVAMDWLRR GRVVVVPGSG FGPHGEGYVR
LCFAASEDTI REALGRLAGI LG
//
