ID A0A059KQT1_9BURK Unreviewed; 383 AA.
AC A0A059KQT1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=X805_09130 {ECO:0000313|EMBL:KDB53458.1};
OS Sphaerotilus natans subsp. natans DSM 6575.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB53458.1, ECO:0000313|Proteomes:UP000026714};
RN [1] {ECO:0000313|EMBL:KDB53458.1, ECO:0000313|Proteomes:UP000026714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB53458.1,
RC ECO:0000313|Proteomes:UP000026714};
RX PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA Park S., Kim D.H., Lee J.H., Hur H.G.;
RT "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL FEMS Microbiol. Ecol. 90:68-77(2014).
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|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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:KDB53458.1}.
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DR EMBL; AZRA01000024; KDB53458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059KQT1; -.
DR STRING; 34103.SAMN05421778_105111; -.
DR PATRIC; fig|1286631.3.peg.901; -.
DR eggNOG; COG0436; Bacteria.
DR Proteomes; UP000026714; Unassembled WGS sequence.
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:SF1; ASPARTATE AMINOTRANSFERASE; 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:KDB53458.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KDB53458.1}.
FT DOMAIN 15..374
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 383 AA; 40902 MW; 65164C3313500629 CRC64;
MIDRVAERKA AGARIISLSA GEPDFDTPVH VQEAAIAAIR AGHTRYTQVA GMRPLREAVA
RKFQEENGMP TRWQATIVCS GGKQVIYNAL AATLNAGDEV IIPAPYWVSY PEMVQLCGAR
AVTVPCPEAT GFKLTPEALS AAITPRTRWL ILNSPSNPTG AVYSAAELLA LAEVLLAHPE
VLVLSDDIYE HLVFTGATFA TMAQVEPRLA GRTLTMNGVS KAYAMTGWRI GFATGPQWLL
EAMEKLQGQQ TSGACSISQH AALAALAGPQ DFVRNTREVF ERRRDAVVQG LNRAFGLRCA
RAAGAFYAFA SCEGLIGRTS AGGRLLATDE DVALALLDEA QVAVMQGSAF GLGPYLRIAY
ALDDASLAQA CNAIRHFCES TTT
//
