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Database: UniProt
Entry: A0A0E9LZ01_9BACT
LinkDB: A0A0E9LZ01_9BACT
Original site: A0A0E9LZ01_9BACT 
ID   A0A0E9LZ01_9BACT        Unreviewed;       385 AA.
AC   A0A0E9LZ01;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=UDP-4-amino-4-deoxy-L-arabinose-oxoglutarate aminotransferase {ECO:0000313|EMBL:GAO30464.1};
GN   ORFNames=JCM15548_12734 {ECO:0000313|EMBL:GAO30464.1};
OS   Geofilum rubicundum JCM 15548.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Geofilum.
OX   NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO30464.1, ECO:0000313|Proteomes:UP000032900};
RN   [1] {ECO:0000313|EMBL:GAO30464.1, ECO:0000313|Proteomes:UP000032900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO30464.1};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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:GAO30464.1}.
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DR   EMBL; BAZW01000023; GAO30464.1; -; Genomic_DNA.
DR   RefSeq; WP_062125480.1; NZ_BAZW01000023.1.
DR   AlphaFoldDB; A0A0E9LZ01; -.
DR   STRING; 1236989.JCM15548_12734; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000032900; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR020026; PseC.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03588; PseC; 1.
DR   PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:GAO30464.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW   Transferase {ECO:0000313|EMBL:GAO30464.1}.
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   385 AA;  43776 MW;  A4C2270774ACC454 CRC64;
     MKPISYGRQF ISDEDINAVI QVLKSDFLTQ GPTIQHFEKE FAKYVDAKYA VAVANGTAAL
     HLSAMALNVQ PGDKWLTTPI TFVASANCIR YCGGEIDFID IDSKTYCIDI VKLEEKLKSV
     PKGTYKGIIP VDFAGYPVNM EEIRSLANDY DLKIIEDACH APGGFFVDNQ GTNQKCGNGQ
     FADLAIFSFH PVKHIATGEG GMITTNNKEL YEKLCLYRTH GITRNEDQMS ENHGGWYYQM
     IELGYNYRLS DIQAALGISQ LSRADIGLNA RQEIAQRYNQ AFTKNDHIQT PFVANEANHA
     YHLYIIQIDD RKGLYEYLRK HNIFSQVHYV PVHTMPYYKN QENTKHDLPI AETYYDHCLS
     LPMYPTLTIN EQNYVIDKVL DFVNS
//
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