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Database: UniProt
Entry: B2VLA4_PODAN
LinkDB: B2VLA4_PODAN
Original site: B2VLA4_PODAN 
ID   B2VLA4_PODAN            Unreviewed;       605 AA.
AC   B2VLA4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-NOV-2023, entry version 59.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:CDP29524.1};
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 6 {ECO:0000313|EMBL:CAP49220.1};
GN   ORFNames=PODANS_5_5460 {ECO:0000313|EMBL:CAP49220.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP49220.1};
RN   [1] {ECO:0000313|EMBL:CAP49220.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP49220.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP49220.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP49220.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP29524.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CU607053; CAP49220.1; -; Genomic_DNA.
DR   EMBL; FO904940; CDP29524.1; -; Genomic_DNA.
DR   RefSeq; XP_001929720.1; XM_001929685.1.
DR   AlphaFoldDB; B2VLA4; -.
DR   STRING; 515849.B2VLA4; -.
DR   GeneID; 6334891; -.
DR   KEGG; pan:PODANSg9227; -.
DR   VEuPathDB; FungiDB:PODANS_5_5460; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_011302_1_0_1; -.
DR   OrthoDB; 35837at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   REGION          173..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  66766 MW;  501D357631A7AD87 CRC64;
     MPAFNLGESI PPHTEHVSNF MAVSVSLPTW RANVGYEEGE DWVVGSMTTG YPRFFIHRSI
     QAFAKDILEK TGRKGLVAFL FPTRQVAARC VSFVKLRAPP AIVSSLEVLH LVLDPANPQS
     KALRGLSPSI SAVICSPEGF SFLKQYWQHT GDGVSSRRAE FCHSLFKDGL LRVDEPPKNT
     AAPMSPKPCR GPKRYQRGGS LDAGKPSTTS QTSTTVPDRE ETSRFLEERF GRNLDVSFVE
     PAKSAIKRRI AGALRSDREL TASPVPEKEM ESNTRGVVNL REDDIYLFPA GMNAIFNAHR
     ALLGARGGLK SVNFGFPYVD TLKILEKFGP GCVFYGNASE ADLDDLEARL KAGERFLGLF
     CEFPGNPLLT CPNLARIREM ADKYDFAVVV DETIGTFANI NVLPFADIVV SSLTKIFSGD
     CNVMGGSAIF NPNSRYYSAL KDFARTGYED TYWPEDVMFM ERNSRDFASR IERINANAEA
     ICDVFRENKL IKAVFYPRDN ESSANYEACK VPGGGYGGLI SVVFHRKEQA VAFYDAVDTA
     KGPSLGTNFT LTSPYVLLAH YQELEWASQF GVDPDLIRIS VGLEDTADIV KVFEAALHVA
     EHGSQ
//
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