OAT_BACAN
ID OAT_BACAN Reviewed; 396 AA.
AC Q81TV3; Q6I237; Q6KVX3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Ornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01689};
DE Short=OAT {ECO:0000255|HAMAP-Rule:MF_01689};
DE EC=2.6.1.13 {ECO:0000255|HAMAP-Rule:MF_01689};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_01689};
GN Name=rocD {ECO:0000255|HAMAP-Rule:MF_01689};
GN OrderedLocusNames=BA_1154, GBAA_1154, BAS1071;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000255|HAMAP-Rule:MF_01689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01689}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01689}.
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DR EMBL; AE016879; AAP25122.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30245.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53394.1; -; Genomic_DNA.
DR RefSeq; NP_843636.1; NC_003997.3.
DR RefSeq; WP_000616649.1; NZ_WXXJ01000044.1.
DR RefSeq; YP_027343.1; NC_005945.1.
DR PDB; 3RUY; X-ray; 2.65 A; A/B=5-396.
DR PDBsum; 3RUY; -.
DR AlphaFoldDB; Q81TV3; -.
DR SMR; Q81TV3; -.
DR STRING; 261594.GBAA_1154; -.
DR DNASU; 1089152; -.
DR EnsemblBacteria; AAP25122; AAP25122; BA_1154.
DR EnsemblBacteria; AAT30245; AAT30245; GBAA_1154.
DR GeneID; 45021168; -.
DR KEGG; ban:BA_1154; -.
DR KEGG; bar:GBAA_1154; -.
DR KEGG; bat:BAS1071; -.
DR PATRIC; fig|198094.11.peg.1134; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_3_9; -.
DR OMA; DVFPRFA; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Proline biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Ornithine aminotransferase"
FT /id="PRO_0000120500"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 106..123
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 155..160
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 228..235
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 257..261
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 308..323
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3RUY"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3RUY"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3RUY"
FT HELIX 381..395
FT /evidence="ECO:0007829|PDB:3RUY"
SQ SEQUENCE 396 AA; 43272 MW; 852B997C0386FAA3 CRC64;
MIQTKDIIEL TDTYGANNYH PLPIVISKAE GVWVEDPEGN RYMDLLSAYS AVNQGHRHPK
IINALIDQAN RVTLTSRAFH SDQLGPWYEK VAKLTNKEMV LPMNTGAEAV ETAIKTARRW
AYDVKKVEAN RAEIIVCEDN FHGRTMGAVS MSSNEEYKRG FGPMLPGIIV IPYGDLEALK
AAITPNTAAF ILEPIQGEAG INIPPAGFLK EALEVCKKEN VLFVADEIQT GLGRTGKVFA
CDWDNVTPDM YILGKALGGG VFPISCAAAN RDILGVFEPG SHGSTFGGNP LACAVSIAAL
EVLEEEKLTE RSLQLGEKLV GQLKEIDNPM ITEVRGKGLF IGIELNEPAR PYCEQLKAAG
LLCKETHENV IRIAPPLVIS EEDLEWAFQK IKAVLS
