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
//