ID M2Q259_CERS8 Unreviewed; 474 AA.
AC M2Q259;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
GN ORFNames=CERSUDRAFT_120246 {ECO:0000313|EMBL:EMD30903.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD30903.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD30903.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD30903.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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:0000256|RuleBase:RU365036};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU365036};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004998, ECO:0000256|RuleBase:RU365036}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; KB445829; EMD30903.1; -; Genomic_DNA.
DR AlphaFoldDB; M2Q259; -.
DR STRING; 914234.M2Q259; -.
DR HOGENOM; CLU_016922_10_3_1; -.
DR OrthoDB; 884390at2759; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR010164; Orn_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU365036};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:EMD30903.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 51480 MW; 5C69786AFD1F3C65 CRC64;
MAPSTITPTT AAEQKTNGAT KRTNPAIARA GGDVHINSGD IIRLEHEHGA HNYHPLPIVF
ESAKGAKVWD PEGREYIDML SAYSAVNQGH CHPKIVAALT EQAQKLTLSS RAFYNSVFGR
FAQKVTAMFG YDMVLPMNTG AEAVETGLKL ARKWAYQKKC VPDGAARIFS AVGNFHGRTL
GVISMSTDPE SRTGFGPYLR GVGPTFEDNG EVREIRYGVI EDLERALELH GKNTAAFLIE
PIQGEAGIVV PPEGYLAQVR ELCTRHNVLL ICDEIQTGLC RTGKMMCFEH DNIRPDIVLL
GKALSGGVYP VSAVLADKDI MLCIQPGEHG STYGGNPLGC AVAMAALDVL VEEKLAARAE
ALGERFRRAV RAINSPLVTE VRGRGLLNAV VIDEHQSARG RTAWQLCLLL KSRGVLAKPT
HVNIIRFAPP LVISESDLDR AVKIIESSLH DLDKLDEIPG EVESEKGHKD TLTL
//
