OAT_SCHPO
ID OAT_SCHPO Reviewed; 438 AA.
AC Q9P7L5; P78805;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ornithine aminotransferase car2;
DE EC=2.6.1.13;
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
GN Name=car2; ORFNames=SPBC21C3.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-438.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=20460254; DOI=10.1074/mcp.m110.000208;
RA Bicho C.C., de Lima Alves F., Chen Z.A., Rappsilber J., Sawin K.E.;
RT "A genetic engineering solution to the 'arginine conversion problem' in
RT stable isotope labeling by amino acids in cell culture (SILAC).";
RL Mol. Cell. Proteomics 9:1567-1577(2010).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Prevents arginine conversion to other amino
CC acids. {ECO:0000269|PubMed:20460254}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB76044.1; -; Genomic_DNA.
DR EMBL; D89154; BAA13816.1; -; mRNA.
DR PIR; T42430; T42430.
DR PIR; T50352; T50352.
DR RefSeq; NP_596588.1; NM_001022508.2.
DR AlphaFoldDB; Q9P7L5; -.
DR SMR; Q9P7L5; -.
DR BioGRID; 277152; 10.
DR STRING; 4896.SPBC21C3.08c.1; -.
DR iPTMnet; Q9P7L5; -.
DR MaxQB; Q9P7L5; -.
DR PaxDb; Q9P7L5; -.
DR PRIDE; Q9P7L5; -.
DR EnsemblFungi; SPBC21C3.08c.1; SPBC21C3.08c.1:pep; SPBC21C3.08c.
DR GeneID; 2540626; -.
DR KEGG; spo:SPBC21C3.08c; -.
DR PomBase; SPBC21C3.08c; car2.
DR VEuPathDB; FungiDB:SPBC21C3.08c; -.
DR eggNOG; KOG1402; Eukaryota.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; Q9P7L5; -.
DR OMA; DVFPRFA; -.
DR PhylomeDB; Q9P7L5; -.
DR Reactome; R-SPO-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00358.
DR PRO; PR:Q9P7L5; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IBA:GO_Central.
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; IMP:PomBase.
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 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 2: Evidence at transcript level;
KW Aminotransferase; Cytoplasm; Nucleus; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..438
FT /note="Ornithine aminotransferase car2"
FT /id="PRO_0000120498"
FT MOD_RES 275
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="F -> S (in Ref. 2; BAA13816)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> A (in Ref. 2; BAA13816)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> D (in Ref. 2; BAA13816)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="A -> T (in Ref. 2; BAA13816)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Y -> N (in Ref. 2; BAA13816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 48247 MW; 4D206590E9E4DC22 CRC64;
MSAESLLHNT FSTEQIEVLE NEYAAHNYHP LPVCFSKAKG AKVWDPEGRE YLDFLSAYSA
VNQGHCHPKI IEALVEQAQR VTLSSRAFYN DKFGPFAKYI TEYFGYEMVI PMNTGAEAVE
TACKLARLWG YKAKKIPTDE AIILSCVDNF HGRTMGIISM STDPDARDNY GPYLPNVGPK
ISGADRVLRY NNIEDLKYYL DTFGPKVAAF LVEPIQGEAG VMVPDDGYLE EAYKLCKAHN
VLFIADEVQT GVARTGKMLC IEHSNVKPDV VILGKAISGG VYPVSAVLSS REIMLNFEPG
THGSTYGGNP LGAAVSIAAL EVVKEEKLTE RAAVLGEKFR TALIECKSPI VQKVRGRGLL
NAVVIDESKT NGRTAWDLCL IMRSRGVLAK PTHGNIIRFS PPLVITEEDL MKGIEVIKKS
LNDLPTIDMT PYAEKPIH
