ID   OAT_EMENI               Reviewed;         454 AA.
AC   Q92413; C8VPG9; Q5BCC0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Ornithine aminotransferase;
DE            EC=2.6.1.13 {ECO:0000269|PubMed:10079330};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase;
GN   Name=otaA; ORFNames=AN1810;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=10079330; DOI=10.1007/s002940050440;
RA   Dzikowska A., Swianiewicz M., Talarczyk A., Wisniewska M., Goras M.,
RA   Scazzocchio C., Weglenski P.;
RT   "Cloning, characterisation and regulation of the ornithine transaminase
RT   (otaA) gene of Aspergillus nidulans.";
RL   Curr. Genet. 35:118-126(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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:10079330};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U74303; AAB18259.2; -; Genomic_DNA.
DR   EMBL; AACD01000029; EAA64975.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85604.1; -; Genomic_DNA.
DR   RefSeq; XP_659414.1; XM_654322.1.
DR   AlphaFoldDB; Q92413; -.
DR   SMR; Q92413; -.
DR   STRING; 162425.CADANIAP00008458; -.
DR   EnsemblFungi; CBF85604; CBF85604; ANIA_01810.
DR   EnsemblFungi; EAA64975; EAA64975; AN1810.2.
DR   GeneID; 2875186; -.
DR   KEGG; ani:AN1810.2; -.
DR   VEuPathDB; FungiDB:AN1810; -.
DR   eggNOG; KOG1402; Eukaryota.
DR   HOGENOM; CLU_016922_10_3_1; -.
DR   InParanoid; Q92413; -.
DR   OMA; DVFPRFA; -.
DR   OrthoDB; 145181at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:AspGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR   GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006591; P:ornithine metabolic process; IEA:EnsemblFungi.
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; IPR010164; Orn_aminotrans.
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   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..454
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000120497"
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        200..201
FT                   /note="AL -> V (in Ref. 1; AAB18259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  49216 MW;  6AF3F2971A20DBA1 CRC64;
     MTSNGTNGSA TAYHASSTQE AIQAENDFAA HNYHPLPVVF ARAQGTSVWD PEGRHYLDFL
     SAYSAVNQGH CHPKLVAALV DQASRLTLSS RAFYNDVFPK FAEMVTKYFG FDMVLPMNTG
     AEAVETGIKI ARKWGYKVKG IPENEAIILS AENNFHGRTM AAISLSSDPE SRENYGPYVP
     NIGCTIPGTE KPITYNDKAA LREAFEKAGS NLAAFLVEPI QGEAGIIVPD DDYLQLARSL
     CDQHNVLLIC DEIQTGIART GKLLCHEWSG IKPDMVLLGK AISGGMYPVS CVLGRKDVML
     TVEPGTHGST YGGNPLACAV AIRALEVVQE ENMVERAEKL GQAFRSGLEA IQNPIIQTVR
     GKGLLNAIVI DESKTNGHTA WDLCMLMKEK GLLAKPTHQN IIRLAPPLVI TEEEIAKALE
     IIKAAVAELP NLKGAAEDKV VPPPEKKVKI TLEN