OAT_BACSU
ID OAT_BACSU Reviewed; 401 AA.
AC P38021;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ornithine aminotransferase;
DE Short=OAT;
DE EC=2.6.1.13 {ECO:0000269|PubMed:7540694};
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
GN Name=rocD {ECO:0000303|PubMed:7540694}; OrderedLocusNames=BSU40340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ORNITHINE
RP AMINOTRANSFERASE AND IN ARGININE CATABOLISM, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=7540694; DOI=10.1006/jmbi.1995.0342;
RA Gardan R., Rapoport G., Debarbouille M.;
RT "Expression of the rocDEF operon involved in arginine catabolism in
RT Bacillus subtilis.";
RL J. Mol. Biol. 249:843-856(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8113162; DOI=10.1128/jb.176.5.1234-1241.1994;
RA Calogero S., Gardan R., Glaser P., Schweitzer J., Rapoport G.,
RA Debarbouille M.;
RT "RocR, a novel regulatory protein controlling arginine utilization in
RT Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional
RT activators.";
RL J. Bacteriol. 176:1234-1241(1994).
RN [5]
RP INDUCTION.
RX PubMed=104957; DOI=10.1128/jb.137.1.189-196.1979;
RA Baumberg S., Harwood C.R.;
RT "Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus
RT subtilis.";
RL J. Bacteriol. 137:189-196(1979).
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000269|PubMed:7540694}.
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:0000269|PubMed:7540694};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Part of the rocDEF operon. Expression is sigma L dependent,
CC induced by arginine, ornithine, ctirulline or proline. Ammonium and
CC glutamine strongly repress induction of the rocD by proline, and only
CC glutamine represses weakly induction by arginine.
CC {ECO:0000269|PubMed:104957, ECO:0000269|PubMed:7540694}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow in minimal
CC medium containing either arginine or ornithine as sole nitrogen source.
CC {ECO:0000269|PubMed:7540694}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X81802; CAA57398.1; -; Genomic_DNA.
DR EMBL; D78193; BAA11293.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16071.1; -; Genomic_DNA.
DR EMBL; L22006; AAA19791.1; -; Unassigned_DNA.
DR PIR; S55793; S55793.
DR RefSeq; NP_391914.1; NC_000964.3.
DR RefSeq; WP_003242970.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P38021; -.
DR SMR; P38021; -.
DR STRING; 224308.BSU40340; -.
DR jPOST; P38021; -.
DR PaxDb; P38021; -.
DR PRIDE; P38021; -.
DR EnsemblBacteria; CAB16071; CAB16071; BSU_40340.
DR GeneID; 937755; -.
DR KEGG; bsu:BSU40340; -.
DR PATRIC; fig|224308.179.peg.4364; -.
DR eggNOG; COG4992; Bacteria.
DR InParanoid; P38021; -.
DR OMA; DVFPRFA; -.
DR PhylomeDB; P38021; -.
DR BioCyc; BSUB:BSU40340-MON; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; IDA:UniProtKB.
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 Amino-acid biosynthesis; Aminotransferase; Arginine metabolism; Cytoplasm;
KW Proline biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Ornithine aminotransferase"
FT /id="PRO_0000120503"
FT MOD_RES 258
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43762 MW; E9AA18FEE5AB9620 CRC64;
MTALSKSKEI IDQTSHYGAN NYHPLPIVIS EALGAWVKDP EGNEYMDMLS AYSAVNQGHR
HPKIIQALKD QADKITLTSR AFHNDQLGPF YEKTAKLTGK EMILPMNTGA EAVESAVKAA
RRWAYEVKGV ADNQAEIIAC VGNFHGRTML AVSLSSEEEY KRGFGPMLPG IKLIPYGDVE
ALRQAITPNT AAFLFEPIQG EAGIVIPPEG FLQEAAAICK EENVLFIADE IQTGLGRTGK
TFACDWDGIV PDMYILGKAL GGGVFPISCI AADREILGVF NPGSHGSTFG GNPLACAVSI
ASLEVLEDEK LADRSLELGE YFKSELESID SPVIKEVRGR GLFIGVELTE AARPYCERLK
EEGLLCKETH DTVIRFAPPL IISKEDLDWA IEKIKHVLRN A
