ID Q9RUH1_DEIRA Unreviewed; 510 AA.
AC Q9RUH1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Ornithine aminotransferase, putative {ECO:0000313|EMBL:AAF10980.1};
GN OrderedLocusNames=DR_1415 {ECO:0000313|EMBL:AAF10980.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF10980.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF10980.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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|RuleBase:RU003560}.
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DR EMBL; AE000513; AAF10980.1; -; Genomic_DNA.
DR PIR; B75399; B75399.
DR RefSeq; NP_295138.1; NC_001263.1.
DR AlphaFoldDB; Q9RUH1; -.
DR STRING; 243230.DR_1415; -.
DR PaxDb; 243230-DR_1415; -.
DR EnsemblBacteria; AAF10980; AAF10980; DR_1415.
DR KEGG; dra:DR_1415; -.
DR PATRIC; fig|243230.17.peg.1611; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_0; -.
DR InParanoid; Q9RUH1; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAF10980.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW Transferase {ECO:0000313|EMBL:AAF10980.1}.
SQ SEQUENCE 510 AA; 55756 MW; 82EE27B82B69FF79 CRC64;
MQFRSRGAPV CRVPARLWRM SLQSPPELPS GFIRTSDVLH ERLTPARARH LDLQYGNEEL
LYGLDVLGLA GPFYRTSPWE LEDEQGVRRI NACGYAALPF GEMPPAITSF MQEFLEHNRA
MTLPQQSSSP WRAALQTNLV KLLSRELPSH SDSQVFFCSS GTEAIEGAMK FAKAWRPEAR
HFISFGSGYH GKTYGSLSLT PNPEYQDVFR PLVPGALTSP YGDLDALKAL VRRAGPDKII
AVVVEPIQGE GGVNIPPPGF LRGLGEFCRS HGIVVIADEI QTGLGRTGHW FESAAQGLDA
DIITLAKPLG GGLVPVGATI VRQPIYKKML GGLSSKRHSN TFGGGALSMA VGLKSLEYLL
ENDLPARSRA LGEQGLARLQ DLQRRFPKLL QAVRGQGLLL AMQFQPVVGL ALPGAIRELV
YEGTAILALR ELHHARVMAN LSLSSKRVVR LSPALDMPQD VFTELMDRVE RFAQLNPNAR
SLVTHTPAPT LLRLATFAAS KPKKRTPSDG
//
