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Database: UniProt
Entry: B9XD79_PEDPL
LinkDB: B9XD79_PEDPL
Original site: B9XD79_PEDPL 
ID   B9XD79_PEDPL            Unreviewed;       415 AA.
AC   B9XD79;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Aminotransferase class I and II {ECO:0000313|EMBL:EEF62025.1};
GN   ORFNames=Cflav_PD6300 {ECO:0000313|EMBL:EEF62025.1};
OS   Pedosphaera parvula (strain Ellin514).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF62025.1, ECO:0000313|Proteomes:UP000003688};
RN   [1] {ECO:0000313|EMBL:EEF62025.1, ECO:0000313|Proteomes:UP000003688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin514 {ECO:0000313|EMBL:EEF62025.1,
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   -!- 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:EEF62025.1}.
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DR   EMBL; ABOX02000006; EEF62025.1; -; Genomic_DNA.
DR   RefSeq; WP_007413777.1; NZ_ABOX02000006.1.
DR   AlphaFoldDB; B9XD79; -.
DR   STRING; 320771.Cflav_PD6300; -.
DR   OMA; YPHMPTG; -.
DR   OrthoDB; 9813612at2; -.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF3; L-GLUTAMINE--4-(METHYLSULFANYL)-2-OXOBUTANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:EEF62025.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF62025.1}.
FT   DOMAIN          46..376
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   415 AA;  45590 MW;  3F978E03F05F521D CRC64;
     MSESYIQNLF AERIGGRQYG KSTAIYKFEK IKRAKRAALA ANPGAEIIDM GVGEPDEMAF
     PEVVDKLHEA ARKPENRGYA DNGDALLKQA GARYLERVCT VKGINPDTEV LHSIGSKAAL
     SILPAALINP GDYVLMTTPG YPVFGTHSKY YGGLVHNLPL TEANNFLPDL DSIPKEILSK
     AKVLVINYPN NPTGASATPA FFAKVVDFAK HNNIVVIHDA AYAALVFNGK PLSFLSIPGA
     KDVGIELHST SKTFNMTGWR CGFVAGNELL VKAYGDVKDN TDSGQFLAIQ HASAYCFDHP
     EITEQIAAKY SRRMDALVQV LRDAGFNARK PQGSFFLYVK APKAAIKNNG ARIEFKNAEE
     ISQWLITEKL ISTVPWDDAC SYLRFSVTFS AKDPTDEKRV VAEIAKRLSD VRFEF
//
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