ID   Y1815_ARCFU             Reviewed;         424 AA.
AC   P56969;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Uncharacterized aminotransferase AF_1815;
DE            EC=2.6.1.-;
GN   OrderedLocusNames=AF_1815;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89433.1; -; Genomic_DNA.
DR   PIR; F69476; F69476.
DR   RefSeq; WP_010879310.1; NC_000917.1.
DR   AlphaFoldDB; P56969; -.
DR   SMR; P56969; -.
DR   STRING; 224325.AF_1815; -.
DR   PRIDE; P56969; -.
DR   EnsemblBacteria; AAB89433; AAB89433; AF_1815.
DR   GeneID; 1485038; -.
DR   KEGG; afu:AF_1815; -.
DR   eggNOG; arCOG00914; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OMA; RHIIARR; -.
DR   OrthoDB; 20774at2157; -.
DR   PhylomeDB; P56969; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..424
FT                   /note="Uncharacterized aminotransferase AF_1815"
FT                   /id="PRO_0000120540"
FT   MOD_RES         259
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  46987 MW;  3B4FA958832C1929 CRC64;
     MGFTGRRGKA EIIEAFSKHV SPYKAKFFSM VGIDFVPARR EGVWYWDLDG RKLMDCHCNG
     GVFNLGHRHP EIVKTLVEAL DELDIGNHHL ISEQRARLAE KLAELMPGDI SRTVFGVGGG
     EAIDFAIKLA RGHTGRKKII YAKGGYHGHT GFALAAGDEK YRKPFEPLAP GFVEVPFGDA
     EAVEKAVDDD TAAVLFETIP ATLGMPLPPE DFYRRVREIC DEKGCLMIMD EVQTGLGRTG
     KMWGIEHYKV VPDVIVTAKG LSGGVYPISA TCFKEGLDDF MAENPFIHVS TFGGAELGCV
     VAEKVLEITS RESFLENVRK TGEALSEILG KLKDEYDFVD EIRQKGLFIG IKMVEEGWGP
     LLSISCYHSG ILAVYANNDT SVMQFLPPLI VGEKEVDYIR EKLAGAMEIA SQRREMVEFI
     RKML