(data stored in SCRATCH zone)

SWISSPROT: D6XXY4_BACIE

ID   D6XXY4_BACIE            Unreviewed;       397 AA.
AC   D6XXY4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
DE            Short=OAT {ECO:0000256|HAMAP-Rule:MF_01689};
DE            EC=2.6.1.13 {ECO:0000256|HAMAP-Rule:MF_01689};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
GN   Name=rocD {ECO:0000256|HAMAP-Rule:MF_01689};
GN   OrderedLocusNames=Bsel_0521 {ECO:0000313|EMBL:ADH98057.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98057.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98057.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC       semialdehyde. {ECO:0000256|HAMAP-Rule:MF_01689}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid
CC         + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877,
CC         ChEBI:CHEBI:35179, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066,
CC         ChEBI:CHEBI:59869; EC=2.6.1.13; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01689};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01689};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01689}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. OAT subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01689}.
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DR   EMBL; CP001791; ADH98057.1; -; Genomic_DNA.
DR   RefSeq; WP_013171486.1; NC_014219.1.
DR   STRING; 439292.Bsel_0521; -.
DR   EnsemblBacteria; ADH98057; ADH98057; Bsel_0521.
DR   KEGG; bse:Bsel_0521; -.
DR   eggNOG; ENOG4105C8Y; Bacteria.
DR   eggNOG; COG4992; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00819; -.
DR   OMA; HSAWDLC; -.
DR   OrthoDB; 572533at2; -.
DR   BioCyc; BSEL439292:G1GLR-549-MONOMER; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR010164; Orn_aminotrans.
DR   InterPro; IPR034757; Ornith_aminotrans_bact.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11986:SF94; PTHR11986:SF94; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XXY4.
DR   SWISS-2DPAGE; D6XXY4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01689};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689,
KW   ECO:0000313|EMBL:ADH98057.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01689};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01689,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01689,
KW   ECO:0000313|EMBL:ADH98057.1}.
FT   MOD_RES     255    255       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01689}.
SQ   SEQUENCE   397 AA;  43901 MW;  F0CA4E95C67BB751 CRC64;
     MTKTMDIIEV TEKYGARNYH PLPIVIAKAE GVWVEDPEGN RYIDMLSAYS AVNQGHRHPK
     IIQALKDQAD RITLTSRAFH NDQLGAFYEK VSKMTNKDMV LPMNTGAEAV ETAVKAVRRW
     AYRVKGVPEN QAEIIVCEEN FHGRTMTAVS LSSNEAYKKD FGPMLPGIKV IPYGDLNALK
     EAITPNTAAF LFEPIQGEAG INMPPEGFLK EAYELCRENR VLYVADEIQC GLARSGKLFA
     CDWEEVEPDM YILGKALGGG VMPISCVAAN EEILGVFEPG SHGSTFGGNP LSCAVSVAAL
     DVIESEQLAE RSLRLGTYFK EQLETLDNPK IREVRGRGLF IGVEMTEAAR PYCEALKEKG
     LLCKETHENV IRFAPPLVIS EEDLDWAIGQ IKDVLKG
//

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