ID B1KUM4_CLOBM Unreviewed; 355 AA.
AC B1KUM4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Alanine racemase, N-terminal domain protein {ECO:0000313|EMBL:ACA54108.1};
GN OrderedLocusNames=CLK_1428 {ECO:0000313|EMBL:ACA54108.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA54108.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA54108.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DSD1 family.
CC {ECO:0000256|ARBA:ARBA00005323}.
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; CP000962; ACA54108.1; -; Genomic_DNA.
DR RefSeq; WP_012342254.1; NC_010520.1.
DR AlphaFoldDB; B1KUM4; -.
DR KEGG; cbl:CLK_1428; -.
DR HOGENOM; CLU_067103_0_0_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0047661; F:amino-acid racemase activity; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR CDD; cd06815; PLPDE_III_AR_like_1; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; NF040742; racem_Orr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF3; LYSINE RACEMASE; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR Pfam; PF14031; D-ser_dehydrat; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 10..223
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT DOMAIN 282..350
FT /note="D-serine dehydratase-like"
FT /evidence="ECO:0000259|Pfam:PF14031"
SQ SEQUENCE 355 AA; 39577 MW; 621F9685798BC8FF CRC64;
MDKSYPCVEI NLKNIAHNIR QLIDLCNMKE IKPVIVTKSF CAEKLVVETI IKEGIKTIAD
ARMKNLMKIQ DLKCEKLLLR IPMKSEVSKV IEYSDVSLNS ELEIIKELSK EARKVNKIHK
IILMVDLGDL REGVLPKDAL STVKEIIKLP NLKFIGLGTN LTCYGGVIPD ENNLGKLLEI
KNQIEKELKI KVSIVSGGNS SSLHIIVNDS MPKGVNQLRI GEAAILGRET AYGQKLNNFY
EDSITLVGEI IELKEKPSMP EGNIGLDAFG NKPSFEDKGI MKRAILALGQ QDIKLDGLIP
KDNEIEILGA SSDHLLLDLT KCENQYKIGD TVEFNMNYGC LLTAMTSEYV TKYSK
//
