ID   S6HPR4_9GAMM            Unreviewed;      1007 AA.
AC   S6HPR4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=M23/M37 peptidase/aminotransferase, class III {ECO:0000313|EMBL:EPJ47077.1};
GN   ORFNames=OFPII_15390 {ECO:0000313|EMBL:EPJ47077.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ47077.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ47077.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EPJ47077.1}.
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DR   EMBL; ASZJ01000080; EPJ47077.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HPR4; -.
DR   PATRIC; fig|1330036.3.peg.1467; -.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; 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:EPJ47077.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014822};
KW   Transferase {ECO:0000313|EMBL:EPJ47077.1}.
FT   DOMAIN          32..259
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          427..525
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1007 AA;  110777 MW;  A4A67341CFFB8745 CRC64;
     MTTYWARVLQ NIWHIEANLT QLDGEFDLNF SVDGEQPAIL KVMRADCDTD FIDLQCSALV
     YLSEHAPEIP IPRIIPTSQQ QLFSHVKGPD GEDRVVWLQQ KIQGQTYANF KPQNLSLISN
     IGQVVGAVDK AWQGFKHPAL QRDFKWNLTT AEWISDELNI IDSAPKKALL SAIAEEFQAL
     KPQLQALEQQ AIHNDVNDYN IIVNGSLTHQ AKVMGLIDLG DMCAGPRICN LAIACAYIVL
     GQTDPEKALE SLVAGYHSKN PLTESELDML WPLLKMRLAV SIVISSLMSK ENPDDPYVVI
     SQAPAWEFLL EHNVNQALIA SRLKVACGFE ISPQAANIRQ WLNSERGNFA AILGQDLQDS
     KVKSLSVEIS TCPQNPFDLT GKEAAELGGE YQADEGVWLG YYNEPRLVYT DDAFKKGVYK
     ASNRRTVHIG VDAFGPAGLE VHTPMAAKVA FAEYRAANLD YGGMVILSHQ TPAGDTFYTL
     YGHLDPQSIA HLSLGQALEK GQVFAALGDL SGNGGWNPHL HFQLALTTTG MGDDWPGVAD
     PDDLPLFNAI CPNPAALLNI ADQKIQYTGT SKAQVLAKRQ AHFGENLKLT YADPVMFLRG
     WRHHLFDEWG RPYLDSYNNV PHVGHAHPRI QAVAADQLLR MNSNTRYLHP AQTAFADKIL
     SKMPSSLEVC FFVNSGTEAN ELALRLSRAH TGGKDIITPN HGYHGNTTGA IDISAYKFNA
     KGGSGQVDWV QLVEVADEYR GSYQKDDPDR ATKYAALVDK AIQAIADAPD NRKLAGFIAE
     TFPSVGGQII PPQGYLAEVY AKIRAAGGVC IADEVQTAFG RLGEYYFAFE QQQVVPDIVV
     MGKPIGNGHP IGVLVTTKEI AESFAKGPEY FSTFGGSNLS CRIGKEVLDI VDDERLMENA
     RIMGDKLRQG LRALQEKHPL IGDVRGYGLF IGLDLVLNQS SKQPATQVAD YVKNRMREHR
     ILMGTEGPAD NILKIRPPLT IEAQDVEMVL QVMDEVLSEA ACLLALN
//