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Database: UniProt/TrEMBL
Entry: S6BXN3_9GAMM
LinkDB: S6BXN3_9GAMM
Original site: S6BXN3_9GAMM 
ID   S6BXN3_9GAMM            Unreviewed;       366 AA.
AC   S6BXN3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-SEP-2017, entry version 32.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:BAN68942.1};
GN   ORFNames=EBS_1011 {ECO:0000313|EMBL:BAN68942.1};
OS   endosymbiont of unidentified scaly snail isolate Monju.
OC   Bacteria; Proteobacteria; Gammaproteobacteria.
OX   NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68942.1, ECO:0000313|Proteomes:UP000015562};
RN   [1] {ECO:0000313|EMBL:BAN68942.1, ECO:0000313|Proteomes:UP000015562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Monju {ECO:0000313|EMBL:BAN68942.1};
RX   PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA   Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S.,
RA   Watanabe T., Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H.,
RA   Nemoto S., Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT   "Allying with armored snails: the complete genome of
RT   gammaproteobacterial endosymbiont.";
RL   ISME J. 8:40-51(2014).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201}.
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DR   EMBL; AP012978; BAN68942.1; -; Genomic_DNA.
DR   RefSeq; WP_052199328.1; NZ_AP012978.1.
DR   EnsemblBacteria; BAN68942; BAN68942; EBS_1011.
DR   KEGG; enm:EBS_1011; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000015562; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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; IPR029066; PLP-binding_barrel.
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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000015562};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:BAN68942.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015562}.
FT   DOMAIN      241    365       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     42     42       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      42     42       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   366 AA;  39333 MW;  66E458C100F440C6 CRC64;
     MPTSITEVAG GACARIDLAA LRHNLGVVRD RAPGRRVMAV IKSQAYGHGM LPVAQALREQ
     VDAFALARID EAVALREAGI DAPLVVLEGP LTADDLGLAR RHDLALVIHD LHQLALLQAD
     MSGGALDCWI KFDTGMHRLG FDPAQADWLL EQLRAPPWLR LAGLMTHLAN ADDLSDTTTE
     TQLARMRTVL PGCGLARSLA NSAGILAWPD SHADWVRPGL MLYGASPLTG RDADALDLRP
     VMTLSAPLLA VRRVPRGEPV GYGGTWRAPE DLSLGVVGIG YGDGYPRHIG QAAQALLRGR
     RLPVVGRVSM DMLMVDLRGL PEARVGDRVT LWGEGLPVDE VARWADTIPY TLFCGVTARV
     ARDYGG
//
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