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Database: UniProt
Entry: W7XVG8_9BACT
LinkDB: W7XVG8_9BACT
Original site: W7XVG8_9BACT 
ID   W7XVG8_9BACT            Unreviewed;       336 AA.
AC   W7XVG8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=JCM21142_1713 {ECO:0000313|EMBL:GAF02085.1};
OS   Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Saccharicrinis.
OX   NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF02085.1, ECO:0000313|Proteomes:UP000019402};
RN   [1] {ECO:0000313|EMBL:GAF02085.1, ECO:0000313|Proteomes:UP000019402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF02085.1,
RC   ECO:0000313|Proteomes:UP000019402};
RA   Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA   Iida T., Darby A., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT   Anaerobe Isolated from Marine Mud.";
RL   Genome Announc. 2:e00206-14(2014).
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|RuleBase:RU000481}.
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:GAF02085.1}.
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DR   EMBL; BAMD01000005; GAF02085.1; -; Genomic_DNA.
DR   RefSeq; WP_027473463.1; NZ_KI912107.1.
DR   AlphaFoldDB; W7XVG8; -.
DR   STRING; 869213.GCA_000517085_04183; -.
DR   eggNOG; COG0079; Bacteria.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000019402; 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; 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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          16..331
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   336 AA;  38515 MW;  1824B0A4C7E61EA3 CRC64;
     MIYGHGDDLY QYDKIHINFS SNVKPGGMDR GLKKHLENSV SDCSSYPEPR AKELELCIEQ
     AYHLPPGSAL VTNGAVEAFY LLAAWKQGCN SLIYYPSFSE YEDACHRYNH KLEFVSNTEL
     QDKVVYGQHL VWLCNPNNPD GKIFRPDTLQ AVVEYNKGTL FVIDEAYIDF VEEDVSMIKW
     LSAYKNLIII RSLTKRFVIP GLRLGYLLAA PDIVAQLEKL IIPWRINILA QKAGMYCLKE
     GCKDGFDLAT ILKESKRLQN EINKVDGFSV VFSDTTFFLV KSRWKASEVK SKLIDKYGIL
     IRDASNFRGL TDEHFRVACQ TPSQNNELIK AFRKWR
//
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