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}.
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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
//