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Database: UniProt
Entry: A0A1B0ZSU2_9RHOB
LinkDB: A0A1B0ZSU2_9RHOB
Original site: A0A1B0ZSU2_9RHOB 
ID   A0A1B0ZSU2_9RHOB        Unreviewed;      1000 AA.
AC   A0A1B0ZSU2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase M23 {ECO:0000313|EMBL:ANP37216.1};
GN   ORFNames=JL2886_02327 {ECO:0000313|EMBL:ANP37216.1};
OS   Phaeobacter gallaeciensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=60890 {ECO:0000313|EMBL:ANP37216.1, ECO:0000313|Proteomes:UP000092565};
RN   [1] {ECO:0000313|EMBL:ANP37216.1, ECO:0000313|Proteomes:UP000092565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL2886 {ECO:0000313|EMBL:ANP37216.1,
RC   ECO:0000313|Proteomes:UP000092565};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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DR   EMBL; CP015124; ANP37216.1; -; Genomic_DNA.
DR   RefSeq; WP_065272067.1; NZ_CP015124.1.
DR   AlphaFoldDB; A0A1B0ZSU2; -.
DR   PATRIC; fig|60890.4.peg.2255; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000092565; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000092565};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          23..262
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          428..527
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1000 AA;  108319 MW;  CC4D6D239E939B6C CRC64;
     MTQAHWAAAF AAHWGIEAEL TRLDGEYDLN FLALAADGSG YIVKAMRPGC AQDLVDMQVQ
     ALDHIARAAP DLPCPRVIRA SNGAAMCAIA DETGAERLVW VINQLPGRCY AKAAPKSDSL
     IHEVGAVLGK TNAALADFQH PGLERDFKWN LMQAGWIADD LDCIADPARR ALLTDIHGAF
     AELAPDLAKL PQQAIHNDAN DYNIIVSGEL SEPRRVSGLI DLGDMCNAPR VCDLAIAAAY
     IVLDHPDPEA ALAALVSGYH SACPLTPAEV DMIWPLLRAR LAVSVVNSTL MGAENPDDPY
     VTISQAPAWR FLEGFDLNAK LVNARLRAAC GLPVVEGADR VLAWLNAERG NFAPLMGTDL
     SDVPMGSLSV ENATWPQNPF DMPLEEAARV GEEYGTGIWL GYYNEPRLIY TAPAFRKGRW
     KASNRRTVHL GVDGFAPAGA PLYAPLAGEV FIVENRAHHL DYGGTIILRH ETPAGDTFYT
     LYGHLDPECC DRLKPGDTVA RGEAFCRLGD PTQNGGWAPH VHFQLAMTTD GIEADWPGVG
     DPDEMYLWHA ICPNPAALMN LPDDKTGYQP TDKGEVLKGR RAHFGGNLSL TYSDPVMLLR
     GWKHHLFDEW GRPYLDAYNN VPHVGHAHPR IQAVAADQLK RMNSNTRYLH PAQVAFAEKV
     LSKLPAPFEV CFFVNSGTEA NELALRLARA HTGAKGMVTP DHGYHGNTTG VIDISAYKFN
     AKGGVGQSDW VELVEVADDY RGSFKRDDAN RAQKFADLVD PAIAKLKDKG HGLAGFIAET
     FPSVGGQIIP PKGYLPAVYE KVRAAGGICI ADEVQTGLGR LGDYYFGFEH QGALPDIVVM
     GKPIGNGHPL GVLVTTRAIA DSFAKGPEFF STFGGSTLSC RIGKEVLDIV DDEGLQQNAK
     AMGDQLMAGL RQLEAKHACV GDVRGMGLFL GLELINADGS EATGICSYVK NRMRDHRILI
     GSEGPKDNIL KIRPPLTIDS DDVEMIVQTL DLILDEVATL
//
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