ID   A0A0B4C1C9_9RHOB        Unreviewed;      1002 AA.
AC   A0A0B4C1C9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M23 {ECO:0000313|EMBL:KIC20575.1};
GN   ORFNames=RA20_08060 {ECO:0000313|EMBL:KIC20575.1};
OS   Leisingera sp. ANG-Vp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC20575.1, ECO:0000313|Proteomes:UP000031177};
RN   [1] {ECO:0000313|Proteomes:UP000031177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:KIC20575.1}.
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DR   EMBL; JWLD01000020; KIC20575.1; -; Genomic_DNA.
DR   RefSeq; WP_039126565.1; NZ_JWLD01000020.1.
DR   AlphaFoldDB; A0A0B4C1C9; -.
DR   STRING; 1577896.RA20_08060; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000031177; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd12797; M23_peptidase; 1.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF01636; APH; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          22..264
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          430..529
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1002 AA;  109584 MW;  85E2A4DF673E2200 CRC64;
     MTLAHWAAAL KQHWGIEAEL TRLDGEYDLN FLAKGADGQG YILKAMRPGC ETWLVDMQVK
     AFEHIAERQP DLPCPRVITS MDGQSLLSIA DEDGKQRLVW LLNQLPGRCY AKAEPKSDAL
     IREIGQVLGG SAKALADFQH KGLERDFKWD LMRAGWITDQ LSCIGDPARR AILEDIAADF
     AKLEPVLSKL PKQAIHNDAN DYNIMVAGDL GAPRRVSGLI DLGDMCAAPR ICDLAIAAAY
     IVLDHPSPEA ALAALVAGYH EVYPLTSAEA DMVWPLLRAR LAVSVVNSTL MAADNPGDPY
     VTISQAPAWR FLEGTALHSG LLNARLRAAC GLPVVEGADR VMAWLEQERG NFAPLMGADL
     ADAPMGSLSV EHSTWPQNPF HMPLEEAAKV GEEFEDNGRI WLGYYHEPRL IYAEPAFRKG
     PWKASDRRTV HLAVDAFAPA GTPMFAPLRG EVFVAEYRAG HLDYGGVIIL RHETPEGDPF
     YTLYGHLNPE FLDRLKPGDV VEKGQEFCRL GDPGQNGGWA PHVHFQLALT TEGIEADWPG
     VGDPDEMYMW RAICPNPAAL LNLPDEKVRY HPTDKGEVLA GRRAHFGGNL SLTYNDPVML
     VRGWKHHLFD EWGRPYLDAY NNVPHVGHAH PRIQAVAADQ LKRMNSNTRY LHPAQTAFAD
     KILSKLPDHF EVCFFVNSGT EANELALRLA RAHTGAKGMV TPDHGYHGNT TGAIDISAYK
     FNKPGGVGQS DWVELVEVAD DYRGSFRRDD PERAQKFAGL VDPAIASLQQ RGHGVAGFIA
     ETFPSVGGQI IPPKGYLPAV YEKIRAAGGI CIADEVQTGL GRLGDYYFGF EHQGALPDIV
     VMGKPIGNGH PLGVLVTTKA IAESFAQGPE FFSTFGGSTL SCRTGKEVLD IVDDEGLQKN
     ARVMGGKLIE ALKALEQKHA CVGDVRGMGL FLGLELINPD GSEATEICSY IKNRMRDHRI
     LIGSEGPKDS ILKIRPPLTI EEADVEMIIT VLDGVLTEVE AA
//