ID Q7MAE1_WOLSU Unreviewed; 390 AA.
AC Q7MAE1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=ASPB {ECO:0000313|EMBL:CAE09461.1};
GN OrderedLocusNames=WS0310 {ECO:0000313|EMBL:CAE09461.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422};
RN [1] {ECO:0000313|EMBL:CAE09461.1, ECO:0000313|Proteomes:UP000000422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC NCTC 11488 / FDC 602W {ECO:0000313|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon JM., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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}.
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DR EMBL; BX571657; CAE09461.1; -; Genomic_DNA.
DR RefSeq; WP_011138262.1; NC_005090.1.
DR AlphaFoldDB; Q7MAE1; -.
DR STRING; 273121.WS0310; -.
DR KEGG; wsu:WS0310; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_7; -.
DR Proteomes; UP000000422; 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: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:CAE09461.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000422};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CAE09461.1}.
FT DOMAIN 29..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 390 AA; 43247 MW; B211FDBE77BA52B6 CRC64;
MYSHRIESLS ESMTIAISTL ARELQSKGKD VISLSAGEPD FETPQVIKDE AIKAIEDGFT
KYTSVAGIPE LLKAIQAKLA RDNHLEYETK EILVSNGAKH SLFNIFQAIV EEGDEVIIPS
PYWVTYPEVV TYCGGKNIFI ETCDASGFKM SAAQLKAALT PKTKALVLTT PSNPTGSVYS
RQELEAIAEV LKGTNVWVVS DEMYEKLVYG VEFTSVASIS EDMLKRTITV NGLSKSAAMT
GWRMGYLATK DKKLIKLMDN LQSQCTSNIC SITQKASIPG LDGRIDPEVE KMRQEFERRR
NFAVDALNAI KGLSVIKPEG AFYLFVNTKA LELDSMQFCK DLLEEEGVAV VPGIGFGMEG
YFRLSFATSM EKIEEGIKRI ARFCEKRERA
//
