ID Q7MAU2_WOLSU Unreviewed; 372 AA.
AC Q7MAU2;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=ASPARTATE AMINOTRANSFERASE {ECO:0000313|EMBL:CAE09197.1};
GN OrderedLocusNames=WS0024 {ECO:0000313|EMBL:CAE09197.1};
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:CAE09197.1, 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|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR EMBL; BX571657; CAE09197.1; -; Genomic_DNA.
DR RefSeq; WP_011137997.1; NC_005090.1.
DR AlphaFoldDB; Q7MAU2; -.
DR STRING; 273121.WS0024; -.
DR KEGG; wsu:WS0024; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_1_7; -.
DR Proteomes; UP000000422; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAE09197.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000422};
KW Transferase {ECO:0000313|EMBL:CAE09197.1}.
FT DOMAIN 23..314
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 372 AA; 40782 MW; F72ED7FA170D55B8 CRC64;
MLLFTPGPTP VPESIRVAMG EPTIHHRTPE FEAIFAKTRA LLQEMLGMSE VLMLASSGTG
AMEACVSSLS AKKALTINSG KFGERFGKIA KALKIPSVEI KNDWDTPVSP AQVMEVLKSD
SEIDAFFIQV CESAGGLRHP VEEIAQAIKA YNPNIMVVAD AITAMGVEKI ETTHIDALIG
GSQKAFMLPP GMSIIGLSAK AVEKIEERDV GYYFNLKTEI KNQRKNTTAW TAPTTLIIGL
GRYLEMAKER GFERIYEETR ARALATQAAM KALGLVIFPK APAVAMTTVI DEESAEGMRK
LLKKEYGVNL AGGQDHLKGK IFRINHMGLI EVYESAWVVN ALELALDRLG KRKFDGSANR
LFLETYYKEL GV
//
