ID   A0A135VWK8_9ARCH        Unreviewed;      1027 AA.
AC   A0A135VWK8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AM324_13055 {ECO:0000313|EMBL:KXH77070.1};
OS   Candidatus Thorarchaeota archaeon SMTZ1-83.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH77070.1, ECO:0000313|Proteomes:UP000070043};
RN   [1] {ECO:0000313|EMBL:KXH77070.1, ECO:0000313|Proteomes:UP000070043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH77070.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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:KXH77070.1}.
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DR   EMBL; LRSK01000072; KXH77070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VWK8; -.
DR   Proteomes; UP000070043; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          40..281
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          452..551
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   1027 AA;  113961 MW;  FE45556AC2124115 CRC64;
     MPYGRGVIKL SSRDPDRPRF TEEDAIRISH RLYGVTGSVQ ELPSERDRNY LVRAESGEEY
     VLKIAAASET RNVLEFQNSA MQHISEYGNR MQCPSVVETS DGEQIASVVD DEGNSHFARM
     LTYLPGNVLA VVKPHSAELL CRLGESIGHM TKALQSFSHP AASREFYWDL RNASTVIEKY
     RSHIDDSERR ALVEHFHQYF TENVVPLLTD LRTSIVHNDA NDYNVIVTKV YPFEEATFGI
     LDFGDMVHTC TVFEVVIAAT YAMLGKDDPI SAAAEVVGGY NSVFPLTELE IGLLFPIIRA
     RLAASVSIAA YQRKLEPDNE YLNISQEQIL VLMRKLKEVH PRFATYSFRH ACGLEPCPQS
     TEVQDWLKRN EKEIGSIVDF NLQETPAVVF DLSVGSQDVQ NLEDLSDIDK FAALVVNKLE
     DAEAQYGVGR YGEARLIYAG GQYESAGETR TVHIAVDLFL ESGTRILAPL DGKVHSYLYN
     KNPLDNGPTI ILEHELGNTG LKLHTLFAHL SEDSLDGLER GKKFKKGQEI AKVGEYPTNG
     GWPPHLHFQL IVDMLGWEGD FFGAAAPSYR DIWTSICPNP NIILGIPADV FPKEGMRKDE
     ILRARESSIG RVLGISYKKP LNIVRGHMQF LYDEMGRRYL DARNNVPHVG HSHPRVVEAL
     SSQAAVLNTN TRYLHENLVH YAKRLREKLP EPLSVCFFVN SGSEANELAL RLAKTHTGHQ
     DLIVIDGAYH GNTGSLVDIS PYKFDGPGGK GAPSHVHKVM TPDVYRGPHK SSDPEVGAKY
     AKYVQEVTDL LKKEEKGLAA FVCEPLMGCA GQIVFPEGYL REAFEHVRAA GGVCIVDEVQ
     VGFGRVGTHF WGFETQGVVP DIITLGKPIG NGHPMGAVVT TPEIARSFET GMEWFSSTGG
     NPVSCAVGLA VLDIIEEEQL QQRALDVGRH LVERLTELKL NHSTIGDVRG IGLFMGVELV
     RDKKTLEPAA EEAAYVANRM RELGVLLSTD GLFHNVLLIK PPLAFSKEDC DLLTDTLDRV
     LSEDFVS
//