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
//