ID S5U487_9EUKA Unreviewed; 392 AA.
AC S5U487;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=SS50377_11958 {ECO:0000313|EMBL:AGS57603.1}, SS50377_24076
GN {ECO:0000313|EMBL:KAH0574130.1};
OS Spironucleus salmonicida.
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Hexamitinae;
OC Spironucleus.
OX NCBI_TaxID=348837 {ECO:0000313|EMBL:AGS57603.1};
RN [1] {ECO:0000313|EMBL:AGS57603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:AGS57603.1};
RA Jerlstrom-Hultqvist J., Einarsson E., Xu F., Hjort K., Ek B., Steinhauf D.,
RA Hultenby K., Bergquist J., Andersson J.O., Svard S.G.;
RT "Hydrogenosomes in the diplomonad Spironucleus salmonicida.";
RL Nat. Commun. 2493:42493-42493(2013).
RN [2] {ECO:0000313|EMBL:KAH0574130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0574130.1};
RX PubMed=24516394;
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 10:E1004053-E1004053(2014).
RN [3] {ECO:0000313|EMBL:EST47938.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 0:0-0(2014).
RN [4] {ECO:0000313|EMBL:KAH0574130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0574130.1};
RA Xu F., Kurt Z., Jimenez-Gonzalez A., Astvaldsson A., Andersson J.O.,
RA Svard S.G.;
RT "New Spironucleus salmonicida genome in near-complete chromosomes.";
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000256|ARBA:ARBA00037974}.
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DR EMBL; KC952881; AGS57603.1; -; Genomic_DNA.
DR EMBL; KI546017; EST47938.1; -; Genomic_DNA.
DR EMBL; AUWU02000004; KAH0574130.1; -; Genomic_DNA.
DR EnsemblProtists; EST47938; EST47938; SS50377_11958.
DR VEuPathDB; GiardiaDB:SS50377_24076; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000018208; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43525; PROTEIN MALY; 1.
DR PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AGS57603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018208};
KW Transferase {ECO:0000313|EMBL:AGS57603.1}.
FT DOMAIN 82..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 392 AA; 44799 MW; CAD21C529B45A2C1 CRC64;
MLKNIDSTQL KLQELFNNST INARNGSYSS KIDLPRAEFN NQNLLSFAKA DFETPTPQPI
QSLLIDHIQK YSSGYSYHPD SLYAAIINWQ QKYFGVNLKK QDIAFIPGVM PGICLALKAI
MNPGDKVTLF TPEYPAFFTL MEANRYIWDS VSIQDDTINF EALDLQLKNS KVLLLSNPHN
PTGKVLSRSE IQKIVQLCNK YDIYLIIDEI WQDITFDVQH QSILKYRSEK TVSFSSGSKS
FNTAGFQLAF ALIEDQSLRR AFQAEQDKSF LNSSNIAGIL ALQTGYEQCD QYLFAWKKYI
AENMDYCSKY LRDNVPQVLT YVPDATCLLM LDFSQVFKNC EEAEQALAKQ NIYLQKGSDF
KFNGVFMRLN CGTSRQELNL CMQAVKRAVE VK
//
