ID A0A3A6TDX2_9GAMM Unreviewed; 392 AA.
AC A0A3A6TDX2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aminotransferase class V-fold PLP-dependent enzyme {ECO:0000313|EMBL:RJY11129.1};
GN ORFNames=D5R81_13510 {ECO:0000313|EMBL:RJY11129.1};
OS Parashewanella spongiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Parashewanella.
OX NCBI_TaxID=342950 {ECO:0000313|EMBL:RJY11129.1, ECO:0000313|Proteomes:UP000273022};
RN [1] {ECO:0000313|EMBL:RJY11129.1, ECO:0000313|Proteomes:UP000273022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22492 {ECO:0000313|EMBL:RJY11129.1,
RC ECO:0000313|Proteomes:UP000273022};
RA Wang G.;
RT "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT Pseudoshewanella and Parashewanella.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:RJY11129.1}.
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DR EMBL; QYYH01000087; RJY11129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A6TDX2; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000273022; 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:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:RJY11129.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000273022};
KW Transferase {ECO:0000313|EMBL:RJY11129.1}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42893 MW; B9DC9FF777CD8FCD CRC64;
MQSKWNIATK AIHAGRNKTT HGDLVSPLHQ SATFAFDSVE QGGARFSGDE SGYIYTRLGN
PTTTELELKM AELEGAESAA ATASGMAAVS AALLANLQVG DHLIASRTVY GCSFALMTHQ
FARFGIEVSL VDFADMRTVE AAIRPNTKVV YCETPVNPHL EVFDLKELTR ISREYELVSI
VDNTFMTPLL QRPLDLGIDM VIHSATKYLN GHGDVIAGIV CGKNEIMNKV KYEILKDIGG
VISPHDAWLI LRGLKTLDVR IQRHCDSAEK VAEFLEGHSK VAKVYYPGLL SHQGYPFLGN
QMSRSGGVIA FELNDNFANT VKFVNQLELF TIAVSLGDAE SLIQHPASMT HSPYTTEARL
ESGITDNLIR ISVGLEAVED IINDLRIGLE KL
//
