ID B9XP88_PEDPL Unreviewed; 438 AA.
AC B9XP88;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=Cflav_PD1278 {ECO:0000313|EMBL:EEF58339.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF58339.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF58339.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF58339.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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|ARBA:ARBA00007441,
CC 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:EEF58339.1}.
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DR EMBL; ABOX02000045; EEF58339.1; -; Genomic_DNA.
DR AlphaFoldDB; B9XP88; -.
DR STRING; 320771.Cflav_PD1278; -.
DR Proteomes; UP000003688; 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
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 ECO:0000313|EMBL:EEF58339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EEF58339.1}.
FT DOMAIN 80..429
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 438 AA; 48559 MW; 79747D7E48FBA974 CRC64;
MNQGRFRSRI EKHIEFEQML SSTFYLRKHR NSHLHSPALP VISFQLFMNY KISHRAASLS
SSLTLAIDSK AKQMKADGLD VVGFGVGEPD FDTPRHIKDA AIKALNEGFT KYTAASGIPE
LRQAIADKFK RDNGLTYKPS QIIVSCGGKH SCYNVIIATC EEGDEVVIPA PYWLSYPEMV
KLAGAKPVIV QTSDKTEFKV TPEQLRAAIT PRTRLFILNS PSNPTGSLYS RDEIKALGDI
CVEKGVLIMS DEIYEKLVYD GAEHVSVASF SKAHYDHTIV VHGFAKAYSM TGWRLGYLAA
PEPIAKAIDA IQSHSTSNPT SFAQKGAVEA LNGPQDHLKT WLEEYAKRRM FAYQKLNSIP
GISCVNAKGA FYLFPNISKL GLNSTDFCAK LLEQEKVAAV PGIAFGTDEY IRISYATSMA
NLEKGLERIE RFAKTLKK
//
