ID A4ADA6_9GAMM Unreviewed; 381 AA.
AC A4ADA6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=2-keto-4-methylthiobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:EAQ96030.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:EAQ96030.1};
GN ORFNames=KT71_12845 {ECO:0000313|EMBL:EAQ96030.1};
OS Congregibacter litoralis KT71.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Congregibacter.
OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ96030.1, ECO:0000313|Proteomes:UP000019205};
RN [1] {ECO:0000313|EMBL:EAQ96030.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ96030.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT "Characterization of a marine gammaproteobacterium capable of aerobic
RT anoxygenic photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN [2] {ECO:0000313|EMBL:EAQ96030.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ96030.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT "The photosynthetic apparatus and its regulation in the aerobic
RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL PLoS ONE 4:E4866-E4866(2009).
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:EAQ96030.1}.
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DR EMBL; AAOA02000001; EAQ96030.1; -; Genomic_DNA.
DR RefSeq; WP_008295000.1; NZ_CM002299.1.
DR AlphaFoldDB; A4ADA6; -.
DR STRING; 314285.KT71_12845; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_0_6; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000019205; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF20; FI04487P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EAQ96030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019205};
KW Transferase {ECO:0000313|EMBL:EAQ96030.1}.
FT DOMAIN 27..378
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 381 AA; 41784 MW; 2E4810FF672F2015 CRC64;
MPLKSKLPQV GTTIFTRMSG LAQTHNALNL SQGFPDFAPP EGLARALGEH AVQGHNQYAP
MAGLPRLREA IAGQLALHRK VTVDPEEEIT VVPGATEGIF CAITAVVEGG DEVIVLDPVY
DSYEPAIALA GGRAVHVPLT AGSFAIDWDR VEEAISPKTK LFMLNSPHNP CGSVVSAADL
DVLALLAEKH DFYVCSDEVY EHLVFDGRQH RSVLQHPVLK ERSFAHFSFG KTLSVTGWKT
GYCVAPPALT AELRKVHQYV AFVAVTPVQH ALADFFEAQP RYPVKLASDY ERRRDLFLSA
LSESRFSWTP TAGSFFQLLD FADISDESDT ALSERWTREI GVASIPVSVF YENPPTQSVL
RFCFAKSDDI LLEAAERLCA I
//