PABC_SCHPO
ID PABC_SCHPO Reviewed; 231 AA.
AC O42951;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Putative aminodeoxychorismate lyase;
DE EC=4.1.3.38;
DE AltName: Full=4-amino-4-deoxychorismate lyase;
DE Short=ADC lyase;
DE Short=ADCL;
GN ORFNames=SPBC19G7.02;
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 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).
CC -!- FUNCTION: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate
CC (PABA) and pyruvate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17056.1; -; Genomic_DNA.
DR PIR; T39833; T39833.
DR RefSeq; NP_595968.1; NM_001021876.2.
DR AlphaFoldDB; O42951; -.
DR SMR; O42951; -.
DR BioGRID; 277187; 2.
DR STRING; 4896.SPBC19G7.02.1; -.
DR MaxQB; O42951; -.
DR PaxDb; O42951; -.
DR EnsemblFungi; SPBC19G7.02.1; SPBC19G7.02.1:pep; SPBC19G7.02.
DR PomBase; SPBC19G7.02; -.
DR VEuPathDB; FungiDB:SPBC19G7.02; -.
DR eggNOG; ENOG502S7GD; Eukaryota.
DR HOGENOM; CLU_020844_6_1_1; -.
DR InParanoid; O42951; -.
DR OMA; RGMIRAK; -.
DR PhylomeDB; O42951; -.
DR UniPathway; UPA00077; UER00150.
DR PRO; PR:O42951; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; ISO:PomBase.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0046656; P:folic acid biosynthetic process; ISO:PomBase.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Folate biosynthesis; Lyase; Nucleus; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..231
FT /note="Putative aminodeoxychorismate lyase"
FT /id="PRO_0000339123"
SQ SEQUENCE 231 AA; 26264 MW; 5FDF6E44ECD5A444 CRC64;
MEESNLFETT LYDGELFLLP SHLQRMKASA KSLGYSWPGE QYIENKLREA VQDTSMARVR
WELSKAGDVT VQIVPIQTLE KAPYTLILDK QPSSTEKNPS CINKMTNRAI YIEAMNRNDA
QYSKAQDVLL YNHQGFVTEA TIFNVAFHRN GQWITPSLKH GLLSGTMRKN LLENGSIHED
DKGLLQKDNL KNGEQVLLFN SFRKVCKGVL IIQPEKACEL LKKKDSSEKL S
