ID   A3X784_9RHOB            Unreviewed;      1002 AA.
AC   A3X784;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=M23/M37 peptidase/aminotransferase, class III {ECO:0000313|EMBL:EAQ46317.1};
GN   ORFNames=MED193_14017 {ECO:0000313|EMBL:EAQ46317.1};
OS   Roseobacter sp. MED193.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ46317.1, ECO:0000313|Proteomes:UP000005943};
RN   [1] {ECO:0000313|EMBL:EAQ46317.1, ECO:0000313|Proteomes:UP000005943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED193 {ECO:0000313|EMBL:EAQ46317.1,
RC   ECO:0000313|Proteomes:UP000005943};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:EAQ46317.1}.
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DR   EMBL; AANB01000002; EAQ46317.1; -; Genomic_DNA.
DR   RefSeq; WP_009810309.1; NZ_CH902583.1.
DR   AlphaFoldDB; A3X784; -.
DR   STRING; 314262.MED193_14017; -.
DR   eggNOG; COG0160; Bacteria.
DR   eggNOG; COG0739; Bacteria.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_010757_1_0_5; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000005943; 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:UniProtKB-KW.
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   Aminotransferase {ECO:0000313|EMBL:EAQ46317.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:EAQ46317.1}.
FT   DOMAIN          21..264
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          430..530
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1002 AA;  109430 MW;  2104DEC647930394 CRC64;
     MNLQHWADAL NSHWGLTADL RRLDGEYDLN FIATDADGTG YILKAMRPGC EAWLVEMQVQ
     AFQHIAAQAP ELPCPRVIPS SNGEAMLSLP DDSGADRLCW VLECLPGKCY ANAAPKTASL
     IHEVGAALGG VGKALADFQH PNLARDFKWD LMQAGWVGSE IDSLSDPSRQ SLIKEIETTF
     ANLEPVLQSL PKQAIHNDAN DYNIMVTGEL TEPRRVSGLI DLGDICAAPR VCDLAIAAAY
     IVLDHLDPEA ALTALVAGYH STYPLTAQEV DLIYPLLRMR LAVSVVNSTL MAAENPDDPY
     VTISQAPAWR FLEGHDLHPG LLSARLRAAC GMPVVEGAER VMDWLNSERG NFAPLMGADL
     KDAPMGSLSV ENSTWPQNPF HMPLQEAARV GEEFEDGDKI WLGYYHEPRL IYTEPAFRKG
     PHKASNRRTV HLAVDAFAPA GTPMFAPLAG EVFVVENRTG HLDYGGVIIL RHETPAGDPF
     YTLYGHLDPE CCERLAQGDQ IEKGAQFCRL GDASMNGGWA PHVHFQLALT TQGIEADWPG
     VGDPDEMYMW RAICPNPAAL LNLPDEKCRY QPTNKDTIRK GRQDHFGDNL SLTYSDPVML
     LRGWKHHLFD EWGRPYLDAY NNVPHVGHAH PRIQAVAADQ LKRMNSNTRY LHPAQTAFAD
     KILSKLPNHL EVCFFVNSGS EANELALRLA RAHTGAKGMV TPDHGYHGNT TGVIDVSAYK
     FNAKGGIGKS DWVELVEVAD DYRGSFKRDD ADRAQKFAEL VDPAIEALQK RGQGVAGFIA
     ETFPSVGGQI IPPRGYLPAV YKKIRAAGGI CIADEVQTGL GRLGDYYFGF EHQGASPDIV
     VMGKPIGNGH PIGVLVTTRA IADSFAKGPE FFSTFGGSTL SCRMGKEVLD IVDDEDLQEN
     ARLMGADLIA GLKALEAKHS CVGDIRGMGL FLGVELINAD GSEATQICAY VKNRMRDHRI
     LIGSEGPKDN ILKIRPPLTI DAEGVQMILT VLDSVLSEVA LP
//