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Database: UniProt
Entry: D6YUA9_WADCW
LinkDB: D6YUA9_WADCW
Original site: D6YUA9_WADCW 
ID   D6YUA9_WADCW            Unreviewed;       386 AA.
AC   D6YUA9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarateaminotransferase {ECO:0000313|EMBL:ADI37720.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ADI37720.1};
GN   Name=arnB {ECO:0000313|EMBL:ADI37720.1};
GN   OrderedLocusNames=wcw_0346 {ECO:0000313|EMBL:ADI37720.1};
OS   Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37720.1, ECO:0000313|Proteomes:UP000001505};
RN   [1] {ECO:0000313|EMBL:ADI37720.1, ECO:0000313|Proteomes:UP000001505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX   PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA   Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA   Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT   "The Waddlia genome: a window into chlamydial biology.";
RL   PLoS ONE 5:E10890-E10890(2010).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP001928; ADI37720.1; -; Genomic_DNA.
DR   RefSeq; WP_013181448.1; NZ_LVEB01000042.1.
DR   AlphaFoldDB; D6YUA9; -.
DR   STRING; 716544.wcw_0346; -.
DR   KEGG; wch:wcw_0346; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_0_3_0; -.
DR   OMA; FKDNPYF; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000001505; Chromosome.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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:ADI37720.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001505};
KW   Transferase {ECO:0000313|EMBL:ADI37720.1}.
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   386 AA;  43060 MW;  98218D4F11E0E679 CRC64;
     MNKKTFLPYG RQSISDDDVQ FVADALRSDW ITRGSKVQEF EEAVAEYCGA RYAVAFSSGT
     SALHAAAHAA KISPYDRVMT TPNTFVASIG PSILKGATPV FVDIDRDTGN LSLEQLKYTL
     EVPFTRGQQV VIPVHFGGIA VDMETLSKAL VHPDSLVIED AAHALGSSYP DGSKVGCCAY
     SAMTVFSFHP VKAITTGEGG MVTTNDFECY QALKQYRNNG IVKPENYPQP WYYEVEELTG
     NHHLTDFQAA LGLSQLGRLD AFAEKRRVLV KRYRQQLKGL PYLSLFTDCA DEDTCFHLMV
     VQIDFEALGK TREGLVEALE QKGIGTQVHY IPIYRHPFFK KKIKDVSAYF PNMEAYYSRA
     LSLPLFAEME ESDVDCVVSE IQRYLC
//
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