ID A5JJJ9_BORBZ Unreviewed; 356 AA.
AC A5JJJ9;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:ABQ43051.1};
DE Flags: Fragment;
GN Name=alr {ECO:0000313|EMBL:ABQ43051.1};
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=445985 {ECO:0000313|EMBL:ABQ43051.1};
RN [1] {ECO:0000313|EMBL:ABQ43051.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZS7 {ECO:0000313|EMBL:ABQ43051.1};
RX PubMed=18598631; DOI=10.3201/eid1407.070880;
RA Qiu W.G., Bruno J.F., McCaig W.D., Xu Y., Livey I., Schriefer M.E.,
RA Luft B.J.;
RT "Wide distribution of a high-virulence Borrelia burgdorferi clone in Europe
RT and North America.";
RL Emerg. Infect. Dis. 14:1097-1104(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
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; EF537497; ABQ43051.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JJJ9; -.
DR GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 242..356
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 36
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ43051.1"
FT NON_TER 356
FT /evidence="ECO:0000313|EMBL:ABQ43051.1"
SQ SEQUENCE 356 AA; 41041 MW; 27EA4422DDE443E6 CRC64;
TMGSNKTIII NLNNLEHNLN LIKNKIGEKE IVATLKGDAY GHGLINIFKF LKSKNINYFG
LSNIEDAKTL KKIDKNIKIL MYIKVDKKEI KNLIKFELVP FVSDFEYLFL IEKECALQKN
KIKVHLKIDI GMNRYGIKID DALEIATYIQ NSKFLELEGI CSHLPSIENF KTTQKQIEQF
LFFLETLKQK NIHPKFVHIS NSGHIINYKL NPQFNMVRPG LILYGYCQSL KNKKPALNFK
PVLSLFSKVI FIKNVKKGEK ISYSGIFQAK EDMKIGIIPI GYFDGIPQNI SNDFYFLINN
KKCKIRGKVC MNLTIVEIPK DLKVKTGSKV EIVSEKLSID EMSKFSKRSH YELLCN
//
