ID   H1YCV8_9SPHI            Unreviewed;       413 AA.
AC   H1YCV8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Aminotransferase class I and II {ECO:0000313|EMBL:EHQ25129.1};
GN   ORFNames=Mucpa_0954 {ECO:0000313|EMBL:EHQ25129.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ25129.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ25129.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ25129.1,
RC   ECO:0000313|Proteomes:UP000002774};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CM001403; EHQ25129.1; -; Genomic_DNA.
DR   RefSeq; WP_008504774.1; NZ_CM001403.1.
DR   AlphaFoldDB; H1YCV8; -.
DR   STRING; 714943.Mucpa_0954; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_10; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000002774; Chromosome.
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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:EHQ25129.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW   Transferase {ECO:0000313|EMBL:EHQ25129.1}.
FT   DOMAIN          32..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   413 AA;  45840 MW;  C605D5B5795D3C87 CRC64;
     MPSISTKGLE MPASPIRKLT PFADKAKQQG KKVYHLNIGQ PDIETPEVML NAIKNIDFKV
     WAYTASEGTL SYRTKLTSYY NKLGYNITPD DIIVTTGGSE AIIITMLTCL NPGDEVIIPE
     PFYANYNGFA CQSDVVVKPI LSYIENGFAL PAISEFEKLI TDKTKGIMIC NPNNPTGYLY
     SPEELEALKE LALKYDLYLF SDEAYREFCY DGRTFTSPMH LDGLDEHVVV LDTVSKRYSA
     CGARLGCMIT KNKAIIASAL KFAQARLSPG MVEQIAGEAA VDTPDEYFEK VNKEYTHRRD
     VLVQALNKMD GVFCPNPGGA FYVVATLPID NADKFCQWIL EEFEYHNQTV MMAPATGFYS
     TPGAGTNQVR MAYVLNADDL QKAMTCLEQA LLVYPGRVAL IPETESAKLN QGQ
//