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
//