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
//