GenomeNet

Database: UniProt
Entry: G3B0P2_CANTC
LinkDB: G3B0P2_CANTC
Original site: G3B0P2_CANTC 
ID   G3B0P2_CANTC            Unreviewed;       428 AA.
AC   G3B0P2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Beta alanine synthase {ECO:0000313|EMBL:EGV65568.1};
GN   ORFNames=CANTEDRAFT_113200 {ECO:0000313|EMBL:EGV65569.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV65569.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 {ECO:0000313|EMBL:EGV65569.1}, and ATCC 10573 / BCRC
RC   21748 / CBS 615 / JCM 9827 / NBRC 10315 / NRRL Y-1498 / VKM Y-70
RC   {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL996514; EGV65568.1; -; Genomic_DNA.
DR   EMBL; GL996514; EGV65569.1; -; Genomic_DNA.
DR   RefSeq; XP_006685254.1; XM_006685191.1.
DR   RefSeq; XP_006685255.1; XM_006685192.1.
DR   GeneID; 18246854; -.
DR   KEGG; cten:CANTEDRAFT_113200; -.
DR   eggNOG; ENOG502QPR4; Eukaryota.
DR   HOGENOM; CLU_024588_2_0_1; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT   DOMAIN          222..323
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   428 AA;  47196 MW;  B5826DDA67E9D34E CRC64;
     MSFQHLKVTP HRLINTIHQT AQWGAKGIWG PEPTQTGMCR LTLSDDDKEV RDWFIKEVNS
     LGCKVKIDQL GNIFAIYSGQ KDGLPTAIGS HLDTQPTGGR YDGILGVLCG LEVLRTIKDN
     GFTPKYPIAV INWTNEEGAR FPVSLMSSLV WSGAHDLQET YNLKSITDDV PVTVRDELER
     IGYIGDVPVD YKQNPIKCHF EIHIEQGPIL EESNKKIGIV VGAQGYDWTK VHVKGKATHT
     GTTPFYARSD ALLATSQMIC KGNELAKKAE GLFSVGVLNL LPKVVNVIPD STEFVMDLRH
     PIKDSLHKLK DDCVEEFKKI AHEAGRNVSV EFEHVMLSDP LEFHADCVSC VQSAAVELYG
     KDNVLEIVSG AGHDSCATSG VVPTSMIFIP SKDGVSHNPE EYSTPEQVAE GFQVLLNAVL
     RYDSLRVD
//
DBGET integrated database retrieval system