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Database: UniProt/TrEMBL
Entry: A0A0K8J4J7_9FIRM
LinkDB: A0A0K8J4J7_9FIRM
Original site: A0A0K8J4J7_9FIRM 
ID   A0A0K8J4J7_9FIRM        Unreviewed;       376 AA.
AC   A0A0K8J4J7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-FEB-2018, entry version 19.
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=alr2 {ECO:0000313|EMBL:CUH92284.1};
GN   ORFNames=SD1D_0736 {ECO:0000313|EMBL:CUH92284.1};
OS   Herbinix luporum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Herbinix.
OX   NCBI_TaxID=1679721 {ECO:0000313|EMBL:CUH92284.1, ECO:0000313|Proteomes:UP000196053};
RN   [1] {ECO:0000313|EMBL:CUH92284.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SD1D {ECO:0000313|EMBL:CUH92284.1};
RA   Rombouts S.;
RT   "Genome analysis of Pseudomonas syringae pv. porri LMG.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|SAAS:SAAS00630646}.
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, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; LN879430; CUH92284.1; -; Genomic_DNA.
DR   RefSeq; WP_058257663.1; NZ_LN879430.1.
DR   KEGG; hsd:SD1D_0736; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000196053; Chromosome i.
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; -; 2.
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; IPR020622; Ala_racemase_pyridoxalP-BS.
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.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196053};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CUH92284.1};
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:UP000196053}.
FT   DOMAIN      248    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED        8     28       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    269    269       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     317    317       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  41952 MW;  AC83F537DE7AB504 CRC64;
     MERCDYYRAQ ANINLEAIRS NINQVKSKLK KDTKLMVIVK ADAYGHGAVE VSKALENDMA
     DAYGVAIIEE AMELRKAGIT KPILILGYTP KEQFDYVVAY DVMQTVFSYD MAADLAKEAK
     KQQKTAKIHI KIDTGMSRIG FKDTIESLNE IKKIAALDGI SIAGIFSHFA RADEIDKSSA
     KQQIKRFDDF CKLVNEAGIH IPIRHMANSA GIIELPCAEY DMVRCGIATY GIYPSEEVDH
     KSIRLTPAME LKSHIIYIKE VQEGCGISYG STFVTKRPTK VATIPVGYAD GYSRNLSNIG
     KVIIRGQYAP IIGRVCMDYF MVDVTDIEGV ICGDVVTLLG RDGERSISVK QLAEWSHSFP
     YELVCTVGRR IPRIYF
//
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